Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O54880
|
RPH3L_RAT
|
MADTIFSSGNDQWVCPNDRQLALRAKLQTGWSVHTYQTEKQRRTQCLSPGEVEVILQVIQRAERLDILEQQRIGRLVERLETMQKNVMGNGVSQCLLCGEMLGFLGSSSVFCKDCRKKVCTKCGIEASPGQKRPLWLCKICSEQREVWKRSGAWFYKGLPKYILPLKTPGRADDPHFRPLPVEPTEPQPQSAEVSRVYTWARGRVVSSDSDSDSDLSSSSLEDRPMPSGIKGTKYDKPRGDSGGSMESPRMGPARPPSHLSGSQSSLGSETGAGATDPQGGTLPRPEPRVSGKRHTWATTHY
| null | null |
exocytosis [GO:0006887]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; intracellular protein transport [GO:0006886]; negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; positive regulation of insulin secretion [GO:0032024]; positive regulation of protein secretion [GO:0050714]; regulation of calcium ion-dependent exocytosis [GO:0017158]; response to xenobiotic stimulus [GO:0009410]; spontaneous neurotransmitter secretion [GO:0061669]
|
presynapse [GO:0098793]; secretory granule [GO:0030141]; synapse [GO:0045202]; transport vesicle membrane [GO:0030658]
|
LIM domain binding [GO:0030274]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267]
|
PF02318;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory vesicle membrane. Note=Recruited to the exocytic secretory vesicles by RAB27A.
| null | null | null | null | null |
FUNCTION: Rab GTPase effector involved in the late steps of regulated exocytosis, both in endocrine and exocrine cells. Regulates the exocytosis of dense-core vesicles in neuroendocrine cells through interaction with RAB27A. Acts as a potential RAB3B effector protein in epithelial cells. {ECO:0000269|PubMed:11134008, ECO:0000269|PubMed:17067543, ECO:0000269|PubMed:9367993}.
|
Rattus norvegicus (Rat)
|
O54885
|
TYOBP_MOUSE
|
MGALEPSWCLLFLPVLLTVGGLSPVQAQSDTFPRCDCSSVSPGVLAGIVLGDLVLTLLIALAVYSLGRLVSRGQGTAEGTRKQHIAETESPYQELQGQRPEVYSDLNTQRQYYR
| null | null |
actin cytoskeleton organization [GO:0030036]; apoptotic cell clearance [GO:0043277]; forebrain development [GO:0030900]; integrin-mediated signaling pathway [GO:0007229]; macrophage activation involved in immune response [GO:0002281]; microglial cell activation involved in immune response [GO:0002282]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of transforming growth factor beta1 production [GO:0032911]; neutrophil activation involved in immune response [GO:0002283]; osteoclast differentiation [GO:0030316]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of macrophage fusion [GO:0034241]; positive regulation of microglial cell mediated cytotoxicity [GO:1904151]; positive regulation of natural killer cell activation [GO:0032816]; positive regulation of osteoclast development [GO:2001206]; positive regulation of receptor localization to synapse [GO:1902685]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of tumor necrosis factor production [GO:0032760]; protein stabilization [GO:0050821]; regulation of osteoclast development [GO:2001204]; response to axon injury [GO:0048678]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stimulatory killer cell immunoglobulin-like receptor signaling pathway [GO:0002222]
|
cell surface [GO:0009986]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
| null |
1.10.287.770;
|
TYROBP family
|
PTM: Tyrosine phosphorylated (PubMed:11754004, PubMed:12426565, PubMed:15728241, PubMed:17086186, PubMed:18691974, PubMed:9490415, PubMed:9852069). Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). {ECO:0000250|UniProtKB:O43914, ECO:0000269|PubMed:11754004, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:9490415, ECO:0000269|PubMed:9852069}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9647200}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (PubMed:15471863, PubMed:9647200). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (PubMed:15728241). Also has an inhibitory role in some cells (PubMed:21727189). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (PubMed:15471863). Required for neutrophil activation mediated by integrin (PubMed:17086186). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Also associates non-covalently with the NK cell receptors KLRA4/LY49D and KLRA8/LY49H which leads to NK cell activation (PubMed:9647200). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (PubMed:18957693). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) which is produced by TREM2 ectodomain shedding (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (PubMed:15728241). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (PubMed:18685038). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (PubMed:25690660). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allostimulatory ability (PubMed:21257958). Negatively regulates B cell proliferation (PubMed:21727189). Required for CSF1-mediated osteoclast cytoskeletal organization (PubMed:18691974). Positively regulates multinucleation during osteoclast development (PubMed:12569157, PubMed:14969392). {ECO:0000250|UniProtKB:O43914, ECO:0000269|PubMed:12569157, ECO:0000269|PubMed:14969392, ECO:0000269|PubMed:15471863, ECO:0000269|PubMed:15728241, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:18685038, ECO:0000269|PubMed:18691974, ECO:0000269|PubMed:18957693, ECO:0000269|PubMed:21257958, ECO:0000269|PubMed:21727189, ECO:0000269|PubMed:25690660, ECO:0000269|PubMed:9647200}.
|
Mus musculus (Mouse)
|
O54888
|
RPA2_RAT
|
MDVDSRWRNLPSGPSLKHLTDPSYAVPPEQQKAALQDLTRAHVDSFNYAVLEGLSHAVQAIPPFEFAFKDERISLTIVDAAISPPAVPKGTICKELNIYPAECRGRRSTYRGKLTADISWAVNGVPKGIIKQFLGXVPIMVKSKLCNLYNLPPQVLIEHHEEAEEMGGYFIINGIEKVIRMLIMPRRNFPIAMIRPKWKSRGLGYTQFGVSIHCVREEHSAVNMNLHYVENGTVMLNFIYRKELFFLPLGFALKALVSFSDYQIFQELIKGKEEDSFFKNSVSQMLRIVMEEGCHTQKQVLDYLGERFRVKLSLPDWYPNAEAAEFLFNQCICIHLKSNTDKFYLLCLMTRKLFALARGECMEDNPDSLVNQEVLTPGQLFLMFLKEKMENWLLSIKIALDKRAQKTNVSINNENLMKIFSMGTELTRPFEYLLATGNLRSKTGLGFMQDSGLCVVADKLNFIRYLSHFRCVHRGADFAKMRTTTVRKLLPESWGFLCPVHTPDGAPCGLLNHLTAVCEVVTKFVYTASIPALLCGLGVTPVDAAPCRPYSDCYPVLLDGVMVGWVDKELAPEVADTLRRFKVLRERRCSSLDGGGPDSHDRKAKPVPRAVPLHHSLQAGEACAEPGAGQRRARWNYGAALHEHCHLRGRGFWWSFHTPGALPSQPAEVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQDRSDNKLYRLQTPQSPLVRPCMYDHYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFIDLSEKFKQGDDSLVFGVKPGDPRVMQKLDNDGLPFIGAKLEFGDPYYGYLNLNTGEGFVVYYKSKENCVVDNIKVCSNDTGSGKFKCVCVTVRVPRNPTIGDKFASRHGQKGILSRLWPAEDMPFTESGMMPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALEYFGEMLKAAGYNFYGTERLYSGISGMELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDKVTNQPIGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHVCVKCGSLLSPLLEKPPPSWSAMRNRKYNCTVCGRSDSIDTVSVPYVFRYFVAELAAMNIKVKLDVI
|
2.7.7.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P08518, ECO:0000250|UniProtKB:P30876}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P08518, ECO:0000250|UniProtKB:P30876};
|
embryo implantation [GO:0007566]; neural crest formation [GO:0014029]; nucleologenesis [GO:0017126]; rRNA transcription [GO:0009303]
|
chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]
|
DNA binding [GO:0003677]; DNA/RNA hybrid binding [GO:0071667]; metal ion binding [GO:0046872]; ribonucleoside binding [GO:0032549]; RNA polymerase I activity [GO:0001054]
|
PF04563;PF04561;PF04565;PF00562;PF04560;
|
2.40.50.150;3.90.1070.20;3.90.1100.10;2.40.270.10;3.90.1800.10;3.90.1110.10;
|
RNA polymerase beta chain family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H9Y6}. Chromosome {ECO:0000250|UniProtKB:P70700}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:Q9H9Y6, ECO:0000269|PubMed:9422795}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000250|UniProtKB:Q9H9Y6, ECO:0000269|PubMed:9422795};
| null | null | null | null |
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (By similarity) (PubMed:9422795). Pol I-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol I pre-initiation complex (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex bound to the core promoter that precedes an rDNA repeat unit. The PIC assembly bends the promoter favoring the formation of the transcription bubble and promoter escape. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Highly processive, assembles in structures referred to as 'Miller trees' where many elongating Pol I complexes queue and transcribe the same rDNA coding regions. At terminator sequences downstream of the rDNA gene, PTRF interacts with Pol I and halts Pol I transcription leading to the release of the RNA transcript and polymerase from the DNA (By similarity) (PubMed:9422795). Forms Pol I active center together with the largest subunit POLR1A/RPA1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and the template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. Has proofreading activity: Pauses and backtracks to allow the cleavage of a missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity is associated with decreased transcription fidelity (By similarity). {ECO:0000250|UniProtKB:P10964, ECO:0000250|UniProtKB:Q9H9Y6, ECO:0000269|PubMed:9422795}.
|
Rattus norvegicus (Rat)
|
O54889
|
RPA1_RAT
|
MLASKHTPWRRLQGISFGMYSAEELKKLSVKSITNPRYVDSLGNPSADGLYDLALGPADSKEVCSTCVQDFNNCSGHLGHIDLPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAAIHLLVCQLKVLDVGALQAVYELERILSRFLEETSDPSAFEIQEELEEYTSKILQNNLLGSQGAHVKNVCESRSKLVAHFWKTHMAAKRCPHCKTGRSVVRKEHNSKLTITYPAMVHKKSGQKDAELPEGAPAAPGIDEAQMGKRGYLTPSSAQEHLFAIWKNEGFFLNYLFSGLDDIGPESSFNPSMFFLDFIVVPPSRYRPINRLGDQMFTNGQTVNLQAVMKDAVLIRKLLAVMAQEQKLPCEMTEITIDKENDSSGAIDRSFLSLLPGQSLTDKLYNIWIRLQSHVNIVFDSDMDKLMLEKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSAVDATQREAVAKQLLTPSTGIPKPQGAKVVCRHVKNGDILLLNRQPTLHRPSIQAHRAHILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGANMTIRGCFFTREQYMELVYRGLTDKVGRVKLFPPAILKPFPLWTGKQVVSTLLINIIPEDYTPLNLTGKAKIGSKAWVKEKPRPVPDFDPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGRVLTCLARLFTAYLQLYRGFTLGVEDILVKPNADVMRQRIIEESTQCGPRAVRAALNLPEAASCDEIQGKWQDAIWRKDQRDFNMIDMKFKEEVNHYSNEINKACMPFGLHRQFPENNLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIRPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVIQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLASNYEVIMKSKHLHEVLSRADPQKVLRHFRAIKKWHHRHSSALLRKGAFLSFSQKIQAAVKALNLEGKTQNGRSPETQQMLQMWHELDEQSRRKYQKRAAPCPDPSLSVWRPDIHFASVSETFEKKIDDYSQEWAAQAEKSHNRSELSLDRLRTLLQLKWQRSLCDPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVFNTKKALRRVKSLKKQLTRVCLGEVLQKVDIQESFCMGEKQNKFRVYELRFQFLPHAYYQQEKCLRPEDILHFMETRFFKLLMEAIKKKNSKASAFRSVNTRRATQKDLDDTEDSGRNRREEERDEEEEGNIVDAEAEEGDADASDTKRKEKQEEEVDYESEEEGEEEEEEDVQEEENIKGEGAHQTHEPDEEEGSGLEEESSQNPPCRHSRPQGAEAMERRIQAVRESHSFIEDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHNAIVYTTKGITRCLLNETINSKNEKEFVLNTEGINLPELFKYSEVLDLRRLYSNDIHAVANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIQSSSSPLQQMTFETSFQFLKQATMMGSHDELKSPSACLVVGKVVKGGTGLFELKQPLR
|
2.7.7.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O95602}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:O95602};
|
negative regulation of protein localization to nucleolus [GO:1904750]; rRNA transcription [GO:0009303]
|
chromosome [GO:0005694]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA/RNA hybrid binding [GO:0071667]; RNA polymerase I activity [GO:0001054]; zinc ion binding [GO:0008270]
|
PF04997;PF00623;PF04983;PF05000;PF04998;
|
1.10.132.30;1.10.357.120;2.40.40.20;3.30.70.2850;6.10.250.2940;3.30.1490.180;4.10.860.120;1.10.274.100;
|
RNA polymerase beta' chain family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:9422795}.
|
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O95602}. Chromosome {ECO:0000250|UniProtKB:O35134}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:O95602}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000250|UniProtKB:O95602};
| null | null | null | null |
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (By similarity). Pol I-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol I pre-initiation complex (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex bound to the core promoter that precedes an rDNA repeat unit. The PIC assembly bends the promoter favoring the formation of the transcription bubble and promoter escape. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Highly processive, assembles in structures referred to as 'Miller trees' where many elongating Pol I complexes queue and transcribe the same rDNA coding regions. At terminator sequences downstream of the rDNA gene, PTRF interacts with Pol I and halts Pol I transcription leading to the release of the RNA transcript and polymerase from the DNA (By similarity). Forms Pol I active center together with the second largest subunit POLR1B/RPA2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and the template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. Has proofreading activity: Pauses and backtracks to allow the cleavage of a missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity is associated with decreased transcription fidelity (By similarity). {ECO:0000250|UniProtKB:O95602, ECO:0000250|UniProtKB:P10964}.
|
Rattus norvegicus (Rat)
|
O54890
|
ITB3_MOUSE
|
MRAQWPGQLWAALLALGALAGVVVGESNICTTRGVNSCQQCLAVSPVCAWCSDETLSQGSPRCNLKENLLKDNCAPESIEFPVSEAQILEARPLSSKGSGSSAQITQVSPQRIALRLRPDDSKIFSLQVRQVEDYPVDIYYLMDLSFSMKDDLSSIQTLGTKLASQMRKLTSNLRIGFGAFVDKPVSPYMYISPPQAIKNPCYNMKNACLPMFGYKHVLTLTDQVSRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVLPNDGHCHIGTDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVSLYQNYSELIPGTTVGVLSDDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCVGLKIGDTVSFSIEAKVRGCPQEKEQSFTIKPVGFKDSLTVQVTFDCDCACQAFAQPSSPRCNNGNGTFECGVCRCDQGWLGSMCECSEEDYRPSQQEECSPKEGQPICSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCNCGDCVCDSDWTGYYCNCTTRTDTCMSTNGLLCSGRGNCECGSCVCVQPGSYGDTCEKCPTCPDACSFKKECVECKKFNRGTLHEENTCSRYCRDDIEQVKELTDTGKNAVNCTYKNEDDCVVRFQYYEDTSGRAVLYVVEEPECPKGPDILVVLLSVMGAILLIGLATLLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT
| null | null |
apolipoprotein A-I-mediated signaling pathway [GO:0038027]; apoptotic cell clearance [GO:0043277]; blood coagulation, fibrin clot formation [GO:0072378]; cell adhesion mediated by integrin [GO:0033627]; cell projection morphogenesis [GO:0048858]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0007044]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cellular response to mechanical stimulus [GO:0071260]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to xenobiotic stimulus [GO:0071466]; embryo implantation [GO:0007566]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; maintenance of postsynaptic specialization structure [GO:0098880]; mesodermal cell differentiation [GO:0048333]; negative chemotaxis [GO:0050919]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of lipid storage [GO:0010888]; negative regulation of lipid transport [GO:0032369]; negative regulation of lipoprotein metabolic process [GO:0050748]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; platelet aggregation [GO:0070527]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway [GO:1900731]; positive regulation of angiogenesis [GO:0045766]; positive regulation of bone resorption [GO:0045780]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of cell migration [GO:0030335]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of glomerular mesangial cell proliferation [GO:0072126]; positive regulation of leukocyte migration [GO:0002687]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of T cell migration [GO:2000406]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of extracellular matrix organization [GO:1903053]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of postsynaptic neurotransmitter receptor diffusion trapping [GO:0150054]; regulation of postsynaptic neurotransmitter receptor internalization [GO:0099149]; regulation of protein localization [GO:0032880]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; regulation of serotonin uptake [GO:0051611]; regulation of trophoblast cell migration [GO:1901163]; response to activity [GO:0014823]; smooth muscle cell migration [GO:0014909]; substrate adhesion-dependent cell spreading [GO:0034446]; symbiont entry into host cell [GO:0046718]
|
alpha9-beta1 integrin-ADAM8 complex [GO:0071133]; alphav-beta3 integrin-HMGB1 complex [GO:0035868]; alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; alphav-beta3 integrin-PKCalpha complex [GO:0035866]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; filopodium membrane [GO:0031527]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; glycinergic synapse [GO:0098690]; integrin alpha9-beta1 complex [GO:0034679]; integrin alphav-beta3 complex [GO:0034683]; integrin complex [GO:0008305]; lamellipodium membrane [GO:0031258]; melanosome [GO:0042470]; microvillus membrane [GO:0031528]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic membrane [GO:0045211]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]; synapse [GO:0045202]; synaptic membrane [GO:0097060]
|
C-X3-C chemokine binding [GO:0019960]; enzyme binding [GO:0019899]; extracellular matrix binding [GO:0050840]; fibrinogen binding [GO:0070051]; fibroblast growth factor binding [GO:0017134]; fibronectin binding [GO:0001968]; identical protein binding [GO:0042802]; insulin-like growth factor I binding [GO:0031994]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; neuregulin binding [GO:0038132]; protease binding [GO:0002020]; protein disulfide isomerase activity [GO:0003756]; protein kinase C binding [GO:0005080]; vascular endothelial growth factor receptor 2 binding [GO:0043184]
|
PF07974;PF18372;PF08725;PF07965;PF00362;PF17205;
|
4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410;
|
Integrin beta chain family
|
PTM: Phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling. {ECO:0000250|UniProtKB:P05106}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05106}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05106}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P05106}. Cell junction, focal adhesion {ECO:0000269|PubMed:29038237}. Postsynaptic cell membrane {ECO:0000269|PubMed:18549786}; Single-pass type I membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:29038237}.
| null | null | null | null | null |
FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIB/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIB/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIB/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIB/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surfaces. Fibrinogen binding enhances SELP expression in activated platelets (PubMed:19332769). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (By similarity). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (By similarity). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (By similarity). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (By similarity). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (By similarity). ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). ITGAV:ITGB3 binds to the Lilrb4a/Gp49b receptor and enhances the Lilrb4a-mediated inhibition of mast cell activation (PubMed:11323698). ITGAV:ITGB3 also suppresses marginal zone B cell antibody production through its interaction with Lilrb4a (PubMed:24935931). In brain, plays a role in synaptic transmission and plasticity (PubMed:18549786, PubMed:29038237). Involved in the regulation of the serotonin neurotransmission, is required to localize to specific compartments within the synapse the serotonin receptor SLC6A4 and for an appropriate reuptake of serotonin (PubMed:29038237). Controls excitatory synaptic strength by regulating GRIA2-containing AMPAR endocytosis, which affects AMPAR abundance and composition (PubMed:18549786). ITGAV:ITGB3 act as a receptor for CD40LG (By similarity). ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and migration to IBSP (By similarity). {ECO:0000250|UniProtKB:P05106, ECO:0000269|PubMed:11323698, ECO:0000269|PubMed:18549786, ECO:0000269|PubMed:19332769, ECO:0000269|PubMed:24935931, ECO:0000269|PubMed:29038237}.
|
Mus musculus (Mouse)
|
O54898
|
CAC1G_RAT
|
MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCSLDYETYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAIGVRAGLLSSPVARSGQEPQPSGSCTRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRVPRASPEIQDRDANGSRRLMLPPPSTPTPSGGPPRGAESVHSFYHADCHLEPVRCQAPPPRCPSEASGRTVGSGKVYPTVHTSPPPEILKDKALVEVAPSPGPPTLTSFNIPPGPFSSMHKLLETQSTGACHSSCKISSPCSKADSGACGPDSCPYCARTGAGEPESADHVMPDSDSEAVYEFTQDAQHSDLRDPHSRRRQRSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEGDATKSESEPDFFSPSVDGDGDRKKRLALVALGEHAELRKSLLPPLIIHTAATPMSHPKSSSTGVGEALGSGSRRTSSSGSAEPGAAHHEMKCPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEDRASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRSSASEHQDCNGKSASGRLARTLRTDDPQLDGDDDNDEGNLSKGERIQAWVRSRLPACCRERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLRRLEKKRRSKEKQMAEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVFESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNLSLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLHTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGVNSTDSPKPGAPHTTAHIGAASGFSLEHPTMVPHPEEVPVPLGPDLLTVRKSGVSRTHSLPNDSYMCRNGSTAERSLGHRGWGLPKAQSGSILSVHSQPADTSCILQLPKDVHYLLQPHGAPTWGAIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLSEVSGPSCPLTRSSSFWGGSSIQVQQRSGIQSKVSKHIRLPAPCPGLEPSWAKDPPETRSSLELDTELSWISGDLLPSSQEEPLFPRDLKKCYSVETQSCRRRPGFWLDEQRRHSIAVSCLDSGSQPRLCPSPSSLGGQPLGGPGSRPKKKLSPPSISIDPPESQGSRPPCSPGVCLRRRAPASDSKDPSVSSPLDSTAASPSPKKDTLSLSGLSSDPTDMDP
| null | null |
action potential [GO:0001508]; artery smooth muscle contraction [GO:0014824]; AV node cell action potential [GO:0086016]; AV node cell to bundle of His cell signaling [GO:0086027]; calcium ion import [GO:0070509]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport into cytosol [GO:0060402]; cardiac muscle cell action potential involved in contraction [GO:0086002]; cellular response to dexamethasone stimulus [GO:0071549]; chemical synaptic transmission [GO:0007268]; membrane depolarization during action potential [GO:0086010]; membrane depolarization during AV node cell action potential [GO:0086045]; membrane depolarization during SA node cell action potential [GO:0086046]; neuronal action potential [GO:0019228]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of atrial cardiac muscle cell membrane depolarization [GO:0060371]; regulation of calcium ion transport [GO:0051924]; regulation of heart rate [GO:0002027]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane potential [GO:0042391]; response to nickel cation [GO:0010045]; SA node cell action potential [GO:0086015]; SA node cell to atrial cardiac muscle cell signaling [GO:0086018]; sodium ion transmembrane transport [GO:0035725]
|
cell body [GO:0044297]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated calcium channel complex [GO:0005891]; voltage-gated sodium channel complex [GO:0001518]
|
low voltage-gated calcium channel activity [GO:0008332]; scaffold protein binding [GO:0097110]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated calcium channel activity involved in AV node cell action potential [GO:0086056]; voltage-gated calcium channel activity involved SA node cell action potential [GO:0086059]; voltage-gated sodium channel activity [GO:0005248]
|
PF00520;
|
1.10.287.70;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1G subfamily
|
PTM: In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43497}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O43497}.
| null | null | null | null | null |
FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1G gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group and are strongly blocked by nickel and mibefradil. A particularity of this type of channels is an opening at quite negative potentials and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes. {ECO:0000269|PubMed:11073957, ECO:0000269|PubMed:9495342}.
|
Rattus norvegicus (Rat)
|
O54901
|
OX2G_MOUSE
|
MGSLVFRRPFCHLSTYSLIWGMAAVALSTAQVEVVTQDERKALHTTASLRCSLKTSQEPLIVTWQKKKAVSPENMVTYSKTHGVVIQPAYKDRINVTELGLWNSSITFWNTTLEDEGCYMCLFNTFGSQKVSGTACLTLYVQPIVHLHYNYFEDHLNITCSATARPAPAISWKGTGTGIENSTESHFHSNGTTSVTSILRVKDPKTQVGKEVICQVLYLGNVIDYKQSLDKGFWFSVPLLLSIVSLVILLVLISILLYWKRHRNQERGESSQGMQRMK
| null | null |
cell-cell adhesion [GO:0098609]; heterotypic cell-cell adhesion [GO:0034113]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of macrophage activation [GO:0043031]; negative regulation of macrophage migration [GO:1905522]; negative regulation of neuroinflammatory response [GO:0150079]; negative regulation of T cell migration [GO:2000405]; regulation of immune response [GO:0050776]; regulation of neuroinflammatory response [GO:0150077]
|
axon [GO:0030424]; cell surface [GO:0009986]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
cell-cell adhesion mediator activity [GO:0098632]; protein binding involved in heterotypic cell-cell adhesion [GO:0086080]
|
PF00047;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O54902
|
NRAM2_RAT
|
MVLDPEEKIPDDGASGDHGDSASLGAINPAYSNSSLPHSTGDSEEPFTTYFDEKIPIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWVLLLATIVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRIILWLMVELAIIGSDMQEVIGSAIAINLLSAGRVPLYGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLRGMFVPSCSGCHTPQVEQAVGIVGAVIMPHNMYLHSALVKSRQVNRANKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFEKTNEQVVEVCRNSSSPHADLFPNDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVILTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSEFSNGIGWRIAGGILVLLVCSINMYFVVVYVQELGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGLSFLDCGRSYHLGLTARPEIYLLNTVDAVSLVSR
| null | null |
cadmium ion transmembrane transport [GO:0070574]; cellular response to hypoxia [GO:0071456]; cellular response to iron ion [GO:0071281]; cellular response to tumor necrosis factor [GO:0071356]; cobalt ion transport [GO:0006824]; copper ion import across plasma membrane [GO:0098705]; copper ion transport [GO:0006825]; dendrite morphogenesis [GO:0048813]; erythrocyte development [GO:0048821]; establishment of localization in cell [GO:0051649]; heme biosynthetic process [GO:0006783]; iron import into cell [GO:0033212]; iron ion transmembrane transport [GO:0034755]; iron ion transport [GO:0006826]; lead ion transport [GO:0015692]; learning or memory [GO:0007611]; manganese ion transport [GO:0006828]; multicellular organismal-level iron ion homeostasis [GO:0060586]; nickel cation transport [GO:0015675]; porphyrin-containing compound biosynthetic process [GO:0006779]; porphyrin-containing compound metabolic process [GO:0006778]; response to cadmium ion [GO:0046686]; response to hypoxia [GO:0001666]; response to iron ion [GO:0010039]; response to lead ion [GO:0010288]; response to manganese ion [GO:0010042]; transition metal ion transport [GO:0000041]
|
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basal part of cell [GO:0045178]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular vesicle [GO:1903561]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]; paraferritin complex [GO:0070826]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]; vacuole [GO:0005773]
|
cadmium ion binding [GO:0046870]; cadmium ion transmembrane transporter activity [GO:0015086]; cobalt ion binding [GO:0050897]; cobalt ion transmembrane transporter activity [GO:0015087]; copper ion binding [GO:0005507]; copper ion transmembrane transporter activity [GO:0005375]; ferrous iron transmembrane transporter activity [GO:0015093]; inorganic cation transmembrane transporter activity [GO:0022890]; iron ion binding [GO:0005506]; iron ion transmembrane transporter activity [GO:0005381]; lead ion transmembrane transporter activity [GO:0015094]; manganese ion binding [GO:0030145]; manganese ion transmembrane transporter activity [GO:0005384]; nickel cation binding [GO:0016151]; nickel cation transmembrane transporter activity [GO:0015099]; solute:proton symporter activity [GO:0015295]; transition metal ion transmembrane transporter activity [GO:0046915]; vanadium ion transmembrane transporter activity [GO:0015100]; zinc ion binding [GO:0008270]
|
PF01566;
| null |
NRAMP family
|
PTM: Ubiquitinated by WWP2. {ECO:0000250|UniProtKB:P49282}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P49281}.
|
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P49282}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:P49282}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:24448823}; Multi-pass membrane protein {ECO:0000255}. Extracellular vesicle membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49281}.
|
CATALYTIC ACTIVITY: [Isoform 2]: Reaction=Fe(2+)(in) + H(+)(in) = Fe(2+)(out) + H(+)(out); Xref=Rhea:RHEA:29579, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:16091957, ECO:0000269|PubMed:29317744, ECO:0000269|PubMed:9242408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29580; Evidence={ECO:0000305|PubMed:29317744}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29581; Evidence={ECO:0000305|PubMed:16091957, ECO:0000305|PubMed:9242408}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=Cd(2+)(out) + H(+)(out) = Cd(2+)(in) + H(+)(in); Xref=Rhea:RHEA:73031, ChEBI:CHEBI:15378, ChEBI:CHEBI:48775; Evidence={ECO:0000269|PubMed:9242408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73032; Evidence={ECO:0000305|PubMed:9242408}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=Co(2+)(out) + H(+)(out) = Co(2+)(in) + H(+)(in); Xref=Rhea:RHEA:73035, ChEBI:CHEBI:15378, ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:9242408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73036; Evidence={ECO:0000305|PubMed:9242408}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=H(+)(in) + Mn(2+)(in) = H(+)(out) + Mn(2+)(out); Xref=Rhea:RHEA:29007, ChEBI:CHEBI:15378, ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:29317744, ECO:0000269|PubMed:9242408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29008; Evidence={ECO:0000305|PubMed:29317744}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29009; Evidence={ECO:0000305|PubMed:9242408}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=H(+)(out) + Zn(2+)(out) = H(+)(in) + Zn(2+)(in); Xref=Rhea:RHEA:71195, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16091957, ECO:0000269|PubMed:9242408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71196; Evidence={ECO:0000305|PubMed:16091957, ECO:0000305|PubMed:9242408}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=H(+)(out) + Ni(2+)(out) = H(+)(in) + Ni(2+)(in); Xref=Rhea:RHEA:73039, ChEBI:CHEBI:15378, ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:9242408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73040; Evidence={ECO:0000305|PubMed:9242408}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:16091957, ECO:0000269|PubMed:9242408}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486, ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:16091957};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 uM for Fe(2+) {ECO:0000269|PubMed:16091957}; KM=1.4 uM for H(+) {ECO:0000269|PubMed:16091957}; KM=1.3 uM for Fe(2+) {ECO:0000269|PubMed:29317744};
| null | null | null |
FUNCTION: Proton-coupled metal ion symporter operating with a proton to metal ion stoichiometry of 1:1 (PubMed:16091957, PubMed:9242408). Selectively transports various divalent metal cations, in decreasing affinity: Cd(2+) > Fe(2+) > Co(2+), Mn(2+) >> Zn(2+), Ni(2+), VO(2+) (By similarity) (PubMed:16091957, PubMed:29317744, PubMed:9242408). Essential for maintenance of iron homeostasis by modulating intestinal absorption of dietary Fe(2+) and TF-associated endosomal Fe(2+) transport in erythroid precursors and other cells (By similarity) (PubMed:9242408). Enables Fe(2+) and Mn(2+) ion entry into mitochondria, and is thus expected to promote mitochondrial heme synthesis, iron-sulfur cluster biogenesis and antioxidant defense (PubMed:29317744). Can mediate uncoupled fluxes of either protons or metal ions. {ECO:0000250|UniProtKB:P49281, ECO:0000250|UniProtKB:P49282, ECO:0000269|PubMed:16091957, ECO:0000269|PubMed:29317744, ECO:0000269|PubMed:9242408}.
|
Rattus norvegicus (Rat)
|
O54904
|
B3GT1_MOUSE
|
MASKVSCLYVLTVVCWASALWYLSITRPTSSYTGSKPFSHLTVARKNFTFGNIRTRPINPHSFEFLINEPNKCEKNIPFLVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSKAKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGGPIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVAELIYKTSLHTRLLHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQISPEEMHRIWNDMSSKKHLRC
|
2.4.1.86
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9417047};
|
galactosylceramide biosynthetic process [GO:0006682]; lipid glycosylation [GO:0030259]; oligosaccharide biosynthetic process [GO:0009312]; protein O-linked glycosylation [GO:0006493]
|
Golgi membrane [GO:0000139]
|
glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity [GO:0047275]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]
|
PF01762;
|
3.90.550.50;
|
Glycosyltransferase 31 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133506; EC=2.4.1.86; Evidence={ECO:0000269|PubMed:9417047}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53433; Evidence={ECO:0000269|PubMed:9417047}; CATALYTIC ACTIVITY: Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:16045, ChEBI:CHEBI:15378, ChEBI:CHEBI:17103, ChEBI:CHEBI:17292, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.86; Evidence={ECO:0000250|UniProtKB:Q9Y5Z6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046; Evidence={ECO:0000250|UniProtKB:Q9Y5Z6};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 mM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9417047}; KM=11.8 mM for GlcNAc-beta-pNP {ECO:0000269|PubMed:9417047};
|
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-alpha-D-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. {ECO:0000269|PubMed:9417047}.
|
Mus musculus (Mouse)
|
O54905
|
B3GT2_MOUSE
|
MLQWRRRHCCFAKMTWSPKRSLLRTPLTGVLSLVFLFAMFLFFNHHDWLPGRPGFKENPVTYTFRGFRSTKSETNHSSLRTIWKEVAPQTLRPHTASNSSNTELSPQGVTGLQNTLSANGSIYNEKGTGHPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNETLAPGIQIIRVFLLGISIKLNGYLQHAIQEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHTPYVMKTDSDMFVNTEYLIHKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFSGDLAEKIFKVSLGIRRLHLEDVYVGICLAKLRVDPVPPPNEFVFNHWRVSYSSCKYSHLITSHQFQPSELIKYWNHLQQNKHNACANAAKEKAGRYRHRKLH
|
2.4.1.86
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9417047};
|
galactosylceramide biosynthetic process [GO:0006682]; oligosaccharide biosynthetic process [GO:0009312]; protein O-linked glycosylation [GO:0006493]
|
Golgi membrane [GO:0000139]
|
glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity [GO:0047275]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]
|
PF19341;PF01762;
|
3.90.550.50;
|
Glycosyltransferase 31 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133506; EC=2.4.1.86; Evidence={ECO:0000269|PubMed:9417047}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53433; Evidence={ECO:0000269|PubMed:9417047}; CATALYTIC ACTIVITY: Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:16045, ChEBI:CHEBI:15378, ChEBI:CHEBI:17103, ChEBI:CHEBI:17292, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.86; Evidence={ECO:0000250|UniProtKB:O43825}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046; Evidence={ECO:0000250|UniProtKB:O43825}; CATALYTIC ACTIVITY: Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside IV(3)-beta-[Gal-beta-(1->3)-GlcNAc]-nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41936, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:78565, ChEBI:CHEBI:142448; Evidence={ECO:0000250|UniProtKB:O43825}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41937; Evidence={ECO:0000250|UniProtKB:O43825};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 mM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9417047}; KM=38.3 mM for GlcNAc-beta-pNP {ECO:0000269|PubMed:9417047};
|
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. {ECO:0000269|PubMed:9417047}.
|
Mus musculus (Mouse)
|
O54907
|
TNF12_MOUSE
|
MAARRSQRRRGRRGEPGTALLAPLVLSLGLALACLGLLLVVVSLGSWATLSAQEPSQEELTAEDRREPPELNPQTEESQDVVPFLEQLVRPRRSAPKGRKARPRRAIAAHYEVHPRPGQDGAQAGVDGTVSGWEETKINSSSPLRYDRQIGEFTVIRAGLYYLYCQVHFDEGKAVYLKLDLLVNGVLALRCLEEFSATAASSPGPQLRLCQVSGLLPLRPGSSLRIRTLPWAHLKAAPFLTYFGLFQVH
| null | null |
angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; extrinsic apoptotic signaling pathway [GO:0097191]; immune response [GO:0006955]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; positive regulation of protein catabolic process [GO:0045732]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; receptor ligand activity [GO:0048018]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form is produced from the membrane form by proteolytic processing. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 12, secreted form]: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O54908
|
DKK1_MOUSE
|
MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH
| null | null |
canonical Wnt signaling pathway [GO:0060070]; cell morphogenesis [GO:0000902]; embryonic limb morphogenesis [GO:0030326]; endoderm development [GO:0007492]; endoderm formation [GO:0001706]; face morphogenesis [GO:0060325]; forebrain development [GO:0030900]; hair follicle development [GO:0001942]; head morphogenesis [GO:0060323]; heart induction [GO:0003129]; learning or memory [GO:0007611]; limb development [GO:0060173]; mesoderm formation [GO:0001707]; motor learning [GO:0061743]; negative regulation of apoptotic process [GO:0043066]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of mesodermal cell fate specification [GO:0042662]; negative regulation of neuron projection development [GO:0010977]; negative regulation of ossification [GO:0030279]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of presynapse assembly [GO:1905607]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; negative regulation of Wnt-Frizzled-LRP5/6 complex assembly [GO:1904723]; positive regulation of gene expression [GO:0010628]; positive regulation of JNK cascade [GO:0046330]; positive regulation of midbrain dopaminergic neuron differentiation [GO:1904958]; regulation of endodermal cell fate specification [GO:0042663]; regulation of neuron apoptotic process [GO:0043523]; regulation of receptor internalization [GO:0002090]; regulation of synapse organization [GO:0050807]; regulation of synaptic transmission, glutamatergic [GO:0051966]; regulation of Wnt signaling pathway [GO:0030111]; response to retinoic acid [GO:0032526]; Wnt signaling pathway [GO:0016055]; Wnt signaling pathway involved in somitogenesis [GO:0090244]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
co-receptor binding [GO:0039706]; low-density lipoprotein particle receptor binding [GO:0050750]; receptor antagonist activity [GO:0048019]
|
PF04706;PF21481;PF21479;
|
2.10.80.10;
|
Dickkopf family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6 (PubMed:18524778). Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity (PubMed:26206087). Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning (PubMed:18505822). {ECO:0000269|PubMed:18505822, ECO:0000269|PubMed:18524778, ECO:0000269|PubMed:26206087}.
|
Mus musculus (Mouse)
|
O54909
|
RDH16_MOUSE
|
MWLYLVALVGLWTLLRFFRVRQVVSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQTSSEIREIYGEKYLASYLKRLNKLDKRCNKDLSGVTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALLYWTSLKPEKAL
|
1.1.1.105; 1.1.1.209; 1.1.1.315; 1.1.1.53
| null |
9-cis-retinoic acid biosynthetic process [GO:0042904]; positive regulation of retinoic acid biosynthetic process [GO:1900054]; retinoic acid metabolic process [GO:0042573]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; steroid metabolic process [GO:0008202]
|
endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; organelle membrane [GO:0031090]
|
11-cis-retinol dehydrogenase [GO:0106429]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; androsterone dehydrogenase activity [GO:0047023]; identical protein binding [GO:0042802]; NAD-retinol dehydrogenase activity [GO:0004745]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
|
PTM: Not glycosylated. {ECO:0000269|PubMed:15355969}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11279029, ECO:0000269|PubMed:15355969, ECO:0000269|PubMed:16223484}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:9407098}.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH; Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228; EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:O75452}; CATALYTIC ACTIVITY: Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273; Evidence={ECO:0000269|PubMed:16223484, ECO:0000269|PubMed:9407098}; CATALYTIC ACTIVITY: Reaction=11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42060, ChEBI:CHEBI:15378, ChEBI:CHEBI:16066, ChEBI:CHEBI:16302, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.315; Evidence={ECO:0000269|PubMed:9407098}; CATALYTIC ACTIVITY: Reaction=13-cis-retinol + NAD(+) = 13-cis-retinal + H(+) + NADH; Xref=Rhea:RHEA:42056, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479, ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:O75452}; CATALYTIC ACTIVITY: Reaction=androsterone + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:20381, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.209; Evidence={ECO:0000269|PubMed:9407098}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence={ECO:0000269|PubMed:9407098};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 uM for 3alpha-hydroxy-5alpha-androstan-17-one (androsterone) {ECO:0000269|PubMed:9407098};
|
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:O75452}.
| null | null |
FUNCTION: Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction. {ECO:0000250|UniProtKB:O75452}.
|
Mus musculus (Mouse)
|
O54912
|
KCNK3_RAT
|
MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPEMIERQRLELRQLELRARYNLSEGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVRYLLHRAKRGLGMRHAEVSMANMVLIGFVSCISTLCIGAAAFSYYERWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTHNGQAGGLGGLSCLSGSLGDGVRPRDPVTCAAAAGGMGVGVGVGGSGFRNVYAEMLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEHSHSSPGGGGRYSDTPSHPCLCSGTQRSAISSVSTGLHSLATFRGLMKRRSSV
| null | null |
cellular response to hypoxia [GO:0071456]; cellular response to zinc ion [GO:0071294]; cochlea development [GO:0090102]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of resting membrane potential [GO:0060075]; response to xenobiotic stimulus [GO:0009410]; stabilization of membrane potential [GO:0030322]
|
plasma membrane [GO:0005886]
|
monoatomic ion channel activity [GO:0005216]; open rectifier potassium channel activity [GO:0005252]; outward rectifier potassium channel activity [GO:0015271]; potassium ion leak channel activity [GO:0022841]; S100 protein binding [GO:0044548]
|
PF07885;
|
1.10.287.70;
|
Two pore domain potassium channel (TC 1.A.1.8) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14649}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14649}.
| null | null | null | null | null |
FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward. {ECO:0000250|UniProtKB:O14649}.
|
Rattus norvegicus (Rat)
|
O54915
|
NR1I2_MOUSE
|
MRPEESWSRVGLVQCEEADSALEEPINVEEEDGGLQICRVCGDKANGYHFNVMTCEGCKGFFRRAMKRNVRLRCPFRKGTCEITRKTRRQCQACRLRKCLESGMKKEMIMSDAAVEQRRALIKRKKREKIEAPPPGGQGLTEEQQALIQELMDAQMQTFDTTFSHFKDFRLPAVFHSGCELPEFLQASLLEDPATWSQIMKDRVPMKISLQLRGEDGSIWNYQPPSKSDGKEIIPLLPHLADVSTYMFKGVINFAKVISYFRDLPIEDQISLLKGATFEMCILRFNTMFDTETGTWECGRLAYCFEDPNGGFQKLLLDPLMKFHCMLKKLQLHKEEYVLMQAISLFSPDRPGVVQRSVVDQLQERFALTLKAYIECSRPYPAHRFLFLKIMAVLTELRSINAQQTQQLLRIQDSHPFATPLMQELFSSTDG
| null | null |
cell differentiation [GO:0030154]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]; xenobiotic transport [GO:0042908]
|
intermediate filament cytoskeleton [GO:0045111]; nuclear body [GO:0016604]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; nuclear receptor activity [GO:0004879]; nuclear receptor binding [GO:0016922]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor that binds and is activated by a variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, endogenous compounds and drugs. Response to specific ligands is species-specific, due to differences in the ligand-binding domain. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes (By similarity). Activated by naturally occurring steroids such as pregnenolone and progesterone, the cholesterol metabolite 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, synthetic glucocorticoids and antiglucocorticoids and 16-alpha-carbonitrile (PCN). {ECO:0000250, ECO:0000269|PubMed:12569201, ECO:0000269|PubMed:19297428}.
|
Mus musculus (Mouse)
|
O54916
|
REPS1_MOUSE
|
MEGLTLSDAEQKYYSDLFSYCDIESTKKVVVNGRVLELFRAAQLPNDVVLQIMELCGATRLGYFGRSQFYIALKLVAVAQSGFPLRVESINTVKDLPLPRFVASKNEQESRLAASYSSDSENQGSYSGVIPPPPGRGQVKKGPGSHDAVQPRPSAEQQEPVSPVVSPQQSPPTSPHTWRKHSRHPSGGNSERPLTGPGPFWSPFGDAQAGSSAGDAVWSGQSPPPPQDNWVSFADTPPTSALLTMHPASVQDQTTVRTVASAATANEIRRQSSSYEDPWKITDEQRQYYVNQFKTIQPDLNGFIPGSAAKEFFTKSKLPILELSHIWELSDFDKDGALTLDEFCAAFHLVVARKNGYDLPEKLPESLMPKLIDLEDSADVGEQPGEVGYSGSPAEAPPSKSPSMPSLNQTWPELNQSSEQWETFSERSSSSQTLTQFDSNIAPADPDTAIVHPVPIRMTPSKIHMQEMELKRTSSDHTNPTSPLLVKPSDLSEENKINSSVKFPSGNTVDGYSSSDSFPSDPEQIGSSVTRQRSHSGTSPDNTAPPPPPPRPQPSHSRSSSLDMNRTFAVTTGQQQAGVVAHPPAVPPRPQPSQAPGPSVHRPVDADGLITHTSTSPQQIPEQPNFADFSQFEVFAASNVSEEQDSEAEKHPEVLPAEKASDPSSSLRAAQADSKAEEKTATNVPANVSKGTTPLAPPPKPVRRRLKSEDELRPDVDEHTQKTGVLAAVLTSQPSIPRSVGKDKKAIQASIRRNKETNTVLARLNSELQQQLKDVLEERISLEVQLEQLRPFSHL
| null | null |
clathrin-dependent synaptic vesicle endocytosis [GO:0150007]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]
|
clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular vesicle [GO:0097708]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
|
calcium ion binding [GO:0005509]; molecular adaptor activity [GO:0060090]; SH3 domain binding [GO:0017124]
|
PF12763;
|
1.10.238.10;
| null |
PTM: EGF stimulates phosphorylation on Tyr-residues.
|
SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}. Note=Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May coordinate the cellular actions of activated EGF receptors and Ral-GTPases.
|
Mus musculus (Mouse)
|
O54917
|
E2F6_MOUSE
|
MSQQRTARRQPSLLVDPAQETVRRRCRDPINVENLLPSKIRINLEENVQYVSMRKALKVKRPRFDVSLVYLTRKFMDLVRSAPGGILDLNKVATKLGVRKRRVYDITNVLDGIELVEKKSKNHIRWIGSDLNNFGAAPQQKKLQAELSDLSAMEDALDELIKDCAQQLLELTDDKENERLAYVTYQDIHGIQAFHEQIVIAVKAPEETRLDVPAPREDSITVHIRSTKGPIDVYLCEVEQNHSNGKTNDGIGASPSKSSHPQCPEKEDEPPQ
| null | null |
cell cycle [GO:0007049]; regulation of transcription by RNA polymerase II [GO:0006357]
|
DNA replication factor A complex [GO:0005662]; MLL1 complex [GO:0071339]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF16421;PF02319;
|
6.10.250.540;1.10.10.10;
|
E2F/DP family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75461}.
| null | null | null | null | null |
FUNCTION: Inhibitor of E2F-dependent transcription (PubMed:9403682). Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' (PubMed:18667754, PubMed:9403682). Has a preference for the 5'-TTTCCCGC-3' E2F recognition site (PubMed:9403682). E2F6 lacks the transcriptional activation and pocket protein binding domains (PubMed:9403682). Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression (By similarity). Represses expression of some meiosis-specific genes, including SLC25A31/ANT4 (PubMed:18667754). May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase (By similarity). {ECO:0000250|UniProtKB:O75461, ECO:0000269|PubMed:18667754, ECO:0000269|PubMed:9403682}.
|
Mus musculus (Mouse)
|
O54918
|
B2L11_MOUSE
|
MAKQPSDVSSECDREGGQLQPAERPPQLRPGAPTSLQTEPQGNPDGEGDRCPHGSPQGPLAPPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMVILQLLRFIFRLVWRRH
| null | null |
apoptotic process involved in embryonic digit morphogenesis [GO:1902263]; B cell homeostasis [GO:0001782]; cell-matrix adhesion [GO:0007160]; developmental pigmentation [GO:0048066]; ear development [GO:0043583]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; in utero embryonic development [GO:0001701]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; kidney development [GO:0001822]; leukocyte homeostasis [GO:0001776]; lymphocyte apoptotic process [GO:0070227]; lymphocyte homeostasis [GO:0002260]; male gonad development [GO:0008584]; mammary gland development [GO:0030879]; meiosis I [GO:0007127]; myeloid cell homeostasis [GO:0002262]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy in response to ER overload [GO:0034263]; positive regulation of cell cycle [GO:0045787]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of lymphocyte apoptotic process [GO:0070230]; positive regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902110]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of T cell apoptotic process [GO:0070234]; post-embryonic development [GO:0009791]; regulation of apoptotic process [GO:0042981]; regulation of developmental pigmentation [GO:0048070]; regulation of organ growth [GO:0046620]; response to endoplasmic reticulum stress [GO:0034976]; spermatogenesis [GO:0007283]; spleen development [GO:0048536]; symbiont-mediated activation of host apoptosis [GO:0052151]; T cell apoptotic process [GO:0070231]; T cell homeostasis [GO:0043029]; thymocyte apoptotic process [GO:0070242]; thymus development [GO:0048538]; tube formation [GO:0035148]
|
Bcl-2 family protein complex [GO:0097136]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]
|
microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]
|
PF08945;PF06773;
| null |
Bcl-2 family
|
PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with TRIM2 and ubiquitination, followed by proteasomal degradation (PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes the protein (PubMed:27013495). {ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}.; PTM: Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation. Conversely, deubiquitination catalyzed by USP27X stabilizes the protein. {ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9430630}; Peripheral membrane protein {ECO:0000269|PubMed:9430630}. Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic membranes.
| null | null | null | null | null |
FUNCTION: Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent. {ECO:0000269|PubMed:9430630}.
|
Mus musculus (Mouse)
|
O54924
|
EXOC8_RAT
|
MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLALLPAAAAGASTGEDTAGAGPRERGAAQAGFLPGPAGVPREGPGTGEEGKQRTLTTLLEKVEGCRDLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAALRAPPPVTSKGSNPFEDEAEEELATPEAEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPSVKELRAKVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGEIGLDLTFIIHALLVKDIQGALLSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMRSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEVILVAVQHVDYSLRCEQDPEKKTFIRQNASFLYDTVLPVVERRFEEGVGKPAKQLQDLRNASRLLRVNPESTTSVV
| null | null |
endosome organization [GO:0007032]; exocytosis [GO:0006887]; extracellular matrix disassembly [GO:0022617]; Golgi to plasma membrane transport [GO:0006893]; protein localization [GO:0008104]; protein transport [GO:0015031]
|
cell leading edge [GO:0031252]; exocyst [GO:0000145]; growth cone [GO:0030426]; late endosome [GO:0005770]; perinuclear region of cytoplasm [GO:0048471]
|
phosphatidylinositol binding [GO:0035091]; small GTPase binding [GO:0031267]
|
PF16528;PF08700;
|
1.20.58.1220;1.20.58.1210;2.30.29.30;
|
EXO84 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12954101}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell projection, growth cone {ECO:0000269|PubMed:12954101}. Cell projection {ECO:0000269|PubMed:21658605}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (PubMed:12954101). Localizes at the leading edge of migrating cells (PubMed:21658605). {ECO:0000250, ECO:0000269|PubMed:12954101, ECO:0000269|PubMed:21658605}.
| null | null | null | null | null |
FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
|
Rattus norvegicus (Rat)
|
O54926
|
SIVA_MOUSE
|
MPKRSCPFADAAPLQLKVHVGLKELSHGVFAERYSREVFERTKQLLFQGARAYRDHISSEDCSVNHLQESLKSGVVGAPQPARGQMLIGPDGRLTRCQAQASEGGLPRTAPIACSSCMRSVDGKAVCSQCERALCGQCVYTCWGCGALACVLCGLADYADDGEKTLCTSCAMFEA
| null |
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Isoform 1 binds 3 zinc ions. Isoform 2 binds 2 zinc ions. {ECO:0000250};
|
extrinsic apoptotic signaling pathway [GO:0097191]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]
|
CD27 receptor binding [GO:0005175]; metal ion binding [GO:0046872]; tumor necrosis factor receptor binding [GO:0005164]; virus receptor activity [GO:0001618]
|
PF05458;
| null | null |
PTM: Phosphorylated by ABL2/ARG in response to oxidative stress. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=In the nucleus, accumulates in dot-like structures. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:9177220}.
|
Mus musculus (Mouse)
|
O54928
|
SOCS5_MOUSE
|
MDKVGKMWNNLKYRCQNLFSHEGGSRNENVEMNPNRCPSVKEKSISLGEAAPQQESSPLRENVALQLGLSPSKTFSRRNQNCAAEIPQVVEISIEKDSDSGATPGTRLARRDSYSRHAPWGGKKKHSCSTKTQSSLDTEKKFGRTRSGLQRRERRYGVSSMQDMDSVSSRAVGSRSLRQRLQDTVGLCFPMRTYSKQSKPLFSNKRKIHLSELMLEKCPFPAGSDLAQKWHLIKQHTAPVSPHSTFFDTFDPSLVSTEDEEDRLRERRRLSIEEGVDPPPNAQIHTFEATAQVNPLYKLGPKLAPGMTEISGDGSAIPQTNCDSEEDSTTLCLQSRRQKQRQVSGDSHAHVSRQGAWKVHTQIDYIHCLVPDLLQITGNPCYWGVMDRYEAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYNRSLHARIEQWNHNFSFDAHDPCVFHSSTVTGLLEHYKDPSSCMFFEPLLTISLNRTFPFSLQYICRAVICRCTTYDGIDGLPLPSMLQDFLKEYHYKQKVRVRWLEREPVKAK
| null | null |
cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cytokine-mediated signaling pathway [GO:0019221]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular signal transduction [GO:0035556]; negative regulation of endothelial cell activation [GO:1904988]; negative regulation of epidermal growth factor-activated receptor activity [GO:0007175]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of monocyte chemotactic protein-1 production [GO:0071638]; negative regulation of signal transduction [GO:0009968]; negative regulation of T-helper 2 cell differentiation [GO:0045629]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of T-helper 1 cell differentiation [GO:0045627]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; vascular endothelial cell response to fluid shear stress [GO:0097699]
|
cytoplasm [GO:0005737]; phosphatidylinositol 3-kinase complex [GO:0005942]
|
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; epidermal growth factor receptor binding [GO:0005154]; kinase inhibitor activity [GO:0019210]; receptor tyrosine kinase binding [GO:0030971]
|
PF00017;PF12610;PF07525;
|
3.30.505.10;
| null |
PTM: Phosphorylated. Phosphorylation is induced by EGF (By similarity). {ECO:0000250}.
| null | null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits for instance EGF signaling by mediating the degradation of the EGF receptor/EGFR. Involved in the regulation of T-helper cell differentiation by inhibiting of the IL4 signaling pathway which promotes differentiation into the Th2 phenotype. Can also partially inhibit IL6 and LIF signaling. {ECO:0000269|PubMed:12242343}.
|
Mus musculus (Mouse)
|
O54931
|
AKAP2_MOUSE
|
MAEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTADGASGWSTVLLQGDELTADPIGTNADMAIQKPPQLSEDANQLRSKQDNCGDSRLEPAASSLSPDHKNMEIGVSVAECKSVPGVTSTPHSKDHSSPFYSPSHNGLLADHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSVTEAEPTEKASGRQVPPHIELSRSPSDRMAEGERANGHSTDQPQDLLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEEDEREKEQFCVRKVRPSEEMIELEKERRELIRSQAVKKNPGIAAKWWNPPQEKTIEEQLDEEHLESHRKYKERKEKRAQQEQLQLQQQQQQQLQQQQLQQQQLQQQQLQQQLQQQQLSTSQPCTAPAAHKHLDGIEHTKEDVVTEQIDFSAARKQFQLMENSRQTLAKGQSTPRLFSIKPYYKPLGSIHSDKPPTILRPATVGGTLEDGGTQAAKEQKAPCVSESQSAGAGPANAATQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDEDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETPSALQENSLADFSLPQTPQTDNPSEGREGVSKSFSDHGFYSPSSTLGDSPSVDDPLEYQAGLLVQNAIQQAIAEQVDKAEAHTSKEGSEQQEPEATVEEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNLPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGGYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVRQSTPSPRAKNAPSLPSRTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGTQRPKNLMQTLMEDYETHKSKRRERMDDSSYTSKLLSCKVTSEVLEATRVNRRKSALALRWEAGIYANQEEEDNE
| null | null |
actin filament organization [GO:0007015]; protein localization [GO:0008104]; regulation of cell shape [GO:0008360]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]
|
apical plasma membrane [GO:0016324]; protein-containing complex [GO:0032991]; side of membrane [GO:0098552]
|
protein domain specific binding [GO:0019904]; protein kinase A binding [GO:0051018]; protein-containing complex binding [GO:0044877]
|
PF03285;
| null | null | null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9497389}; Lipid-anchor, GPI-like-anchor {ECO:0000269|PubMed:9497389}; Cytoplasmic side {ECO:0000269|PubMed:9497389}. Note=Accumulates near the inner, apical surface of highly polarized epithelium in tubules of nephrons. {ECO:0000269|PubMed:9497389}.
| null | null | null | null | null |
FUNCTION: Binds to regulatory subunit (RII) of protein kinase A (PubMed:9497389). May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (PubMed:9497389). Binds tp and modulates the structure of the actin cytoskeleton (PubMed:9497389). {ECO:0000269|PubMed:9497389}.
|
Mus musculus (Mouse)
|
O54937
|
PDK4_RAT
|
MKAARFVMRSASSLGNAGLVPREVELFSRYSPSPLSMKQLLDFGSENACERTSFSFLRQELPVRLANILKEIDILPEHLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQKVLSDFVDTLVKVRNRHHNVVPTMAQGILEYKDNCTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDSKTGNPSHIGSIDPNCDVVAVVEDAFECAKMLCDQYYLTSPELKLTQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRPFLTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMDNSRNAPLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLKALSSESIEKLPVFNKSAFKHYQMSSEADDWCIPSKEPKNLSKEKLAV
|
2.7.11.2
| null |
acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; cellular response to fatty acid [GO:0071398]; cellular response to starvation [GO:0009267]; glucose homeostasis [GO:0042593]; insulin receptor signaling pathway [GO:0008286]; negative regulation of anoikis [GO:2000811]; phosphorylation [GO:0016310]; reactive oxygen species metabolic process [GO:0072593]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; regulation of bone resorption [GO:0045124]; regulation of cellular ketone metabolic process [GO:0010565]; regulation of fatty acid biosynthetic process [GO:0042304]; regulation of fatty acid oxidation [GO:0046320]; regulation of glucose metabolic process [GO:0010906]; regulation of pH [GO:0006885]; response to starvation [GO:0042594]
|
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; pyruvate dehydrogenase (acetyl-transferring) kinase activity [GO:0004740]
|
PF10436;PF02518;
|
1.20.140.20;3.30.565.10;
|
PDK/BCKDK protein kinase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit]; Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2; Evidence={ECO:0000269|PubMed:11486000, ECO:0000269|PubMed:9405293};
| null | null | null | null |
FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism. {ECO:0000269|PubMed:11486000}.
|
Rattus norvegicus (Rat)
|
O54939
|
DHB3_RAT
|
MEQFLLSVGLLVCLVCLVKCVRFSRYLFLSFCKALPGSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQVISEEIERTTGSRVKVVQADFTREDIYDHIEEQLKGLEIGVLVNNVGMLPNLLPSHFLSTSGESQSVIHCNITSVVKMTQLVLKHMESRRRGLILNISSGVGVRPWPLYSLYSASKAFVCTFSKALNVEYRDKGIIIQVLTPYSVSTPMTKYLNTSRVTKTADEFVKESLKYVTIGAETCGCLAHEILAIILNLIPSRIFYSSTTQRFLLKQFSDYLKSNISNR
|
1.1.1.62; 1.1.1.64
| null |
biphenyl metabolic process [GO:0018879]; cellular response to antibiotic [GO:0071236]; cellular response to gonadotropin stimulus [GO:0071371]; cellular response to hormone stimulus [GO:0032870]; hippocampus development [GO:0021766]; insecticide metabolic process [GO:0017143]; Leydig cell differentiation [GO:0033327]; organic acid metabolic process [GO:0006082]; phenol-containing compound metabolic process [GO:0018958]; response to activity [GO:0014823]; response to arsenic-containing substance [GO:0046685]; response to cadmium ion [GO:0046686]; response to corticosterone [GO:0051412]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to fatty acid [GO:0070542]; response to fungicide [GO:0060992]; response to herbicide [GO:0009635]; response to insecticide [GO:0017085]; response to L-ascorbic acid [GO:0033591]; response to lead ion [GO:0010288]; response to metal ion [GO:0010038]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]; response to steroid hormone [GO:0048545]; response to vitamin E [GO:0033197]; steroid biosynthetic process [GO:0006694]; testosterone biosynthetic process [GO:0061370]
|
endoplasmic reticulum [GO:0005783]
|
17-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0072582]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; testosterone 17-beta-dehydrogenase (NADP+) activity [GO:0047045]; testosterone dehydrogenase (NAD+) activity [GO:0047035]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family, 17-beta-HSD 3 subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P37058}.
|
CATALYTIC ACTIVITY: Reaction=a 17beta-hydroxy steroid + NADP(+) = a 17-oxo steroid + H(+) + NADPH; Xref=Rhea:RHEA:69284, ChEBI:CHEBI:15378, ChEBI:CHEBI:19168, ChEBI:CHEBI:35343, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69286; Evidence={ECO:0000250|UniProtKB:P37058}; CATALYTIC ACTIVITY: Reaction=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.64; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14983; Evidence={ECO:0000250|UniProtKB:P37058}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24618; Evidence={ECO:0000250|UniProtKB:P37058}; CATALYTIC ACTIVITY: Reaction=3beta-hydroxyandrost-5-en-17-one + H(+) + NADPH = androst-5-en-3beta,17beta-diol + NADP(+); Xref=Rhea:RHEA:46628, ChEBI:CHEBI:2710, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46629; Evidence={ECO:0000250|UniProtKB:P37058}; CATALYTIC ACTIVITY: Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = 5alpha-androstan-3,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:42120, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42122; Evidence={ECO:0000250|UniProtKB:P37058}; CATALYTIC ACTIVITY: Reaction=androsterone + H(+) + NADPH = 5alpha-androstane-3alpha,17beta-diol + NADP(+); Xref=Rhea:RHEA:42156, ChEBI:CHEBI:15378, ChEBI:CHEBI:16032, ChEBI:CHEBI:36713, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42157; Evidence={ECO:0000250|UniProtKB:P37058}; CATALYTIC ACTIVITY: Reaction=3beta-hydroxy-5alpha-androstan-17-one + H(+) + NADPH = 5alpha-androstane-3beta,17beta-diol + NADP(+); Xref=Rhea:RHEA:53480, ChEBI:CHEBI:15378, ChEBI:CHEBI:18329, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:541975; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53481; Evidence={ECO:0000250|UniProtKB:P37058}; CATALYTIC ACTIVITY: Reaction=androst-4-ene-3,11,17-trione + H(+) + NADPH = 17beta-hydroxyandrost-4-ene-3,11-dione + NADP(+); Xref=Rhea:RHEA:53484, ChEBI:CHEBI:2495, ChEBI:CHEBI:15378, ChEBI:CHEBI:34133, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53485; Evidence={ECO:0000250|UniProtKB:P37058}; CATALYTIC ACTIVITY: Reaction=11beta-hydroxyandrost-4-ene-3,17-dione + H(+) + NADPH = 11beta,17beta-dihydroxyandrost-4-ene-3-one + NADP(+); Xref=Rhea:RHEA:53488, ChEBI:CHEBI:15378, ChEBI:CHEBI:27967, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:81481; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53489; Evidence={ECO:0000250|UniProtKB:P37058};
| null |
PATHWAY: Hormone biosynthesis; testosterone biosynthesis. {ECO:0000250|UniProtKB:P37058}.; PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:P37058}.
| null | null |
FUNCTION: Catalyzes the conversion of 17-oxosteroids to 17beta-hydroxysteroids. Favors the reduction of androstenedione to testosterone. Testosterone is the key androgen driving male development and function (By similarity). Uses NADPH while the two other EDH17B enzymes use NADH. Androgens such as epiandrosterone, dehydroepiandrosterone, androsterone and androstanedione are accepted as substrates and reduced at C-17. Can reduce 11-ketoandrostenedione as well as 11beta-hydroxyandrostenedione at C-17 to the respective testosterone forms (By similarity). Plays a role in the rate-limiting-step for the maximum level of testosterone production by the testis but does not affect basal testosterone production (By similarity). {ECO:0000250|UniProtKB:P37058, ECO:0000250|UniProtKB:P70385}.
|
Rattus norvegicus (Rat)
|
O54940
|
BNIP2_MOUSE
|
MEGVELKEEWQDEDFPIPLPEDDSIEADTLDGTDPDRQPGSLEVNGNKVRKKLMAPDISLTLDPGEDSLWSDDLDEAGEVDLEGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYTATEEKGDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQEPPKSEQ
| null | null |
apoptotic process [GO:0006915]; blastocyst development [GO:0001824]; centrosome cycle [GO:0007098]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of small GTPase mediated signal transduction [GO:0051057]; striated muscle cell differentiation [GO:0051146]
|
centriole [GO:0005814]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]; spindle pole centrosome [GO:0031616]
| null |
PF12496;PF13716;
|
3.40.525.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O54941
|
SMCE1_MOUSE
|
MSKRPSYAPPPTPAPATQMPSTPGFVGYNPYSHLAYNNYRLGGNPGTNSRVTASSGITIPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQSSMAPEEEQVANKAEEKKDEESIPMETEETHLEDTAESQQNGEEGTSTPEDKESGQEGVDSMEVEGTSDSNTGSESNSATVEEPPTDPVPEDEKKE
| null | null |
chromatin remodeling [GO:0006338]; negative regulation of DNA-templated transcription [GO:0045892]; neurogenesis [GO:0022008]; nucleosome disassembly [GO:0006337]; positive regulation of cell differentiation [GO:0045597]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of T cell differentiation [GO:0045582]; regulation of G0 to G1 transition [GO:0070316]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357]
|
bBAF complex [GO:0140092]; brahma complex [GO:0035060]; chromatin [GO:0000785]; kinetochore [GO:0000776]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514]
|
N-acetyltransferase activity [GO:0008080]; nuclear receptor binding [GO:0016922]; nucleosomal DNA binding [GO:0031492]; RNA binding [GO:0003723]
|
PF00505;
|
1.10.30.10;
| null |
PTM: Ubiquitinated by TRIP12, leading to its degradation by the proteasome. Ubiquitination is prevented upon interaction between TRIP12 and SMARCC1 (By similarity). {ECO:0000250|UniProtKB:Q969G3}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
| null | null | null | null | null |
FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:12110891). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells (By similarity). Required for the coactivation of estrogen responsive promoters by SWI/SNF complexes and the SRC/p160 family of histone acetyltransferases (HATs) (PubMed:12145209). {ECO:0000250|UniProtKB:Q969G3, ECO:0000269|PubMed:12110891, ECO:0000269|PubMed:12145209, ECO:0000269|PubMed:17640523}.
|
Mus musculus (Mouse)
|
O54942
|
CLD5_MOUSE
|
MGSAALEILGLVLCLVGWVGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYESVLALSAEVQAARALTVGAVLLALVALFVTLTGAQCTTCVAPGPVKARVALTGGALYAVCGLLALVPLCWFANIVVREFYDPTVPVSQKYELGAALYIGWAASALLMCGGGLVCCGAWVCTGRPEFSFPVKYSAPRRPTANGDYDKKNYV
| null | null |
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; establishment of blood-retinal barrier [GO:1990963]; maintenance of blood-brain barrier [GO:0035633]; myelination [GO:0042552]; negative regulation of angiogenesis [GO:0016525]; negative regulation of cell migration [GO:0030336]; negative regulation of gene expression [GO:0010629]; negative regulation of vascular permeability [GO:0043116]; positive regulation of bicellular tight junction assembly [GO:1903348]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of establishment of endothelial barrier [GO:1903142]; positive regulation of gene expression [GO:0010628]; response to ethanol [GO:0045471]; tight junction assembly [GO:0120192]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
apicolateral plasma membrane [GO:0016327]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; lateral plasma membrane [GO:0016328]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; Schmidt-Lanterman incisure [GO:0043220]; tight junction [GO:0070160]
|
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]
|
PF00822;
|
1.20.140.150;
|
Claudin family
| null |
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000269|PubMed:9892664}.
| null | null | null | null | null |
FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O54943
|
PER2_MOUSE
|
MNGYVDFSPSPTSPTKEPGAPQPTQAVLQEDVDMSSGSSGNENCSTGRDSQGSDCDDNGKELRMLVESSNTHPSPDDAFRLMMTEAEHNPSTSGCSSEQSAKADAHKELIRTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSESQPCSVDVPSYSMEQVEGITSEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAKFVEFLAPHDVSVFHSYTTPYKLPPWSVCSGLDSFTQECMEEKSFFCRVSVGKHHENEIRYQPFRMTPYLVKVQEQQGAESQLCCLLLAERVHSGYEAPRIPPEKRIFTTTHTPNCLFQAVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQAGGQPFDYSPIRFRTRNGEYITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAAPPCPEEKTPHPSVQELTEQIHRLLMQPVPHSGSSGYGSLGSNGSHEHLMSQTSSSDSNGQEESHRRRSGIFKTSGKIQTKSHVSHESGGQKEASVAEMQSSPPAQVKAVTTIERDSSGASLPKASFPEELAYKNQPPCSYQQISCLDSVIRYLESCSEAATLKRKCEFPANIPSRKATVSPGLHSGEAARPSKVTSHTEVSAHLSSLTLPGKAESVVSLTSQCSYSSTIVHVGDKKPQPELETVEDMASGPESLDGAAGGLSQEKGPLQKLGLTKEVLAAHTQKEEQGFLQRFREVSRLSALQAHCQNYLQERSRAQASDRGLRNTSGLESSWKKTGKNRKLKSKRVKTRDSSESTGSGGPVSHRPPLMGLNATAWSPSDTSQSSCPSAPFPTAVPAYPLPVFQAPGIVSTPGTVVAPPAATHTGFTMPVVPMGTQPEFAVQPLPFAAPLAPVMAFMLPSYPFPPATPNLPQAFLPSQPHFPAHPTLASEITPASQAEFPSRTSTLRQPCACPVTPPAGTVALGRASPPLFQSRGSSPLQLNLLQLEEAPEGSTGAAGTLGTTGTAASGLDCTSGTSRDRQPKAPPTCNEPSDTQNSDAISTSSDLLNLLLGEDLCSATGSALSRSGASATSDSLGSSSLGFGTSQSGAGSSDTSHTSKYFGSIDSSENNHKAKMIPDTEESEQFIKYVLQDPIWLLMANTDDSIMMTYQLPSRDLQAVLKEDQEKLKLLQRSQPRFTEGQRRELREVHPWVHTGGLPTAIDVTGCVYCESEEKGNICLPYEEDSPSPGLCDTSEAKEEEGEQLTGPRIEAQT
| null | null |
chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; circadian regulation of translation [GO:0097167]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; fatty acid metabolic process [GO:0006631]; gluconeogenesis [GO:0006094]; glycogen biosynthetic process [GO:0005978]; lactate biosynthetic process [GO:0019249]; negative regulation of circadian rhythm [GO:0042754]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fat cell proliferation [GO:0070345]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of termination of DNA-templated transcription [GO:0060567]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription regulatory region DNA binding [GO:2000678]; positive regulation of cold-induced thermogenesis [GO:0120162]; regulation of cell cycle [GO:0051726]; regulation of circadian rhythm [GO:0042752]; regulation of glutamate uptake involved in transmission of nerve impulse [GO:0051946]; regulation of insulin secretion [GO:0050796]; regulation of neurogenesis [GO:0050767]; regulation of vasoconstriction [GO:0019229]; response to ischemia [GO:0002931]; white fat cell differentiation [GO:0050872]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
DNA-binding transcription factor binding [GO:0140297]; histone deacetylase binding [GO:0042826]; histone methyltransferase binding [GO:1990226]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; nuclear receptor binding [GO:0016922]; pre-mRNA binding [GO:0036002]; RNA polymerase binding [GO:0070063]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]; transcription coactivator activity [GO:0003713]; transcription corepressor binding [GO:0001222]
|
PF08447;PF21353;PF12114;
|
3.30.450.20;
| null |
PTM: Acetylated (PubMed:18662546, PubMed:30782483). Deacetylated by SIRT1, resulting in decreased protein stability (PubMed:18662546). Deacetylated by SIRT6, preventing its degradation by the proteasome, resulting in increased protein stability (PubMed:30782483). {ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:30782483}.; PTM: Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. May be dephosphorylated by PP1. {ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:16097765, ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:21930935}.; PTM: Ubiquitinated, leading to its proteasomal degradation. Ubiquitination may be inhibited by CRY1. {ECO:0000269|PubMed:11889036}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:22208286}. Cytoplasm {ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:22208286}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22274616}. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization (PubMed:22274616). {ECO:0000269|PubMed:22274616}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like BMAL1 or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:16595674, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:17404161, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:19917250, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:22504074, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:23977055, ECO:0000269|PubMed:24413057}.
|
Mus musculus (Mouse)
|
O54946
|
DNJB6_MOUSE
|
MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDDEQDRQRVPGNWDAPMTSAGLKEGGKRKKQKQKEDLKKKKSTKGNH
| null | null |
actin cytoskeleton organization [GO:0030036]; chaperone-mediated protein folding [GO:0061077]; chorio-allantoic fusion [GO:0060710]; chorion development [GO:0060717]; extracellular matrix organization [GO:0030198]; intermediate filament organization [GO:0045109]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of inclusion body assembly [GO:0090084]; protein localization to nucleus [GO:0034504]; regulation of protein localization [GO:0032880]; syncytiotrophoblast cell differentiation involved in labyrinthine layer development [GO:0060715]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]
|
ATPase activator activity [GO:0001671]; DNA binding [GO:0003677]; Hsp70 protein binding [GO:0030544]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF00226;
|
1.10.287.110;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
| null | null | null | null | null |
FUNCTION: Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70 (PubMed:18373498). Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250|UniProtKB:O75190, ECO:0000269|PubMed:18373498}.
|
Mus musculus (Mouse)
|
O54947
|
HAVR1_RAT
|
MVQLQVFISGLLLLLPGSVDSYEVVKGVVGHPVTIPCTYSTRGGITTTCWGRGQCPYSSCQNILIWTNGYQVTYRSSGRYNIKGRISEGDVSLTIENSVDSDSGLYCCRVEIPGWFNDQKMTFSLEVKPEIPTSPPTRPTTTRPTTTRPTTISTRSTHVPTSTRVSTSTPTPEQTQTHKPEITTFYAHETTAEVTETPSYTPADWNGTVTSSEEAWNNHTVRIPLRKPQRNPTKGFYVGMSVAALLLLLLASTVVVTRYIIIRKKMGSLSFVAFHVSKSRALQNAAIVHPRAEDNIYIIEDRSRGAE
| null | null |
phagocytosis, engulfment [GO:0006911]; positive regulation of mast cell activation [GO:0033005]; response to lipopolysaccharide [GO:0032496]; response to mycotoxin [GO:0010046]; response to nutrient [GO:0007584]; response to testosterone [GO:0033574]; response to wounding [GO:0009611]; response to xenobiotic stimulus [GO:0009410]
|
apical plasma membrane [GO:0016324]; brush border [GO:0005903]; cell surface [GO:0009986]; extracellular space [GO:0005615]; motile cilium [GO:0031514]; phagocytic vesicle [GO:0045335]
|
phosphatidylserine binding [GO:0001786]; virus receptor activity [GO:0001618]
|
PF07686;
|
2.60.40.10;
|
Immunoglobulin superfamily, TIM family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96D42}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q96D42}.
| null | null | null | null | null |
FUNCTION: Phosphatidylserine receptor that plays an important functional role in regulatory B-cells homeostasis including generation, expansion and suppressor functions (By similarity). As P-selectin/SELPLG ligand, plays a specialized role in activated but not naive T-cell trafficking during inflammatory responses. Controls thereby T-cell accumulation in the inflamed central nervous system (CNS) and the induction of autoimmune disease (By similarity). Regulates also expression of various anti-inflammatory cytokines and co-inhibitory ligands including IL10. Acts as a regulator of T-cell proliferation (By similarity). May play a role in kidney injury and repair (By similarity). {ECO:0000250|UniProtKB:Q5QNS5, ECO:0000250|UniProtKB:Q96D42}.
|
Rattus norvegicus (Rat)
|
O54949
|
NLK_MOUSE
|
MSLCGTRANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPVTNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE
|
2.7.11.24
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
cellular response to osmotic stress [GO:0071470]; intracellular signal transduction [GO:0035556]; negative regulation of TORC1 signaling [GO:1904262]; negative regulation of Wnt signaling pathway [GO:0030178]; peptidyl-threonine phosphorylation [GO:0018107]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of DNA-templated transcription [GO:0006355]; serine phosphorylation of STAT protein [GO:0042501]; transforming growth factor beta receptor signaling pathway [GO:0007179]; Wnt signaling pathway [GO:0016055]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; SH2 domain binding [GO:0042169]; ubiquitin protein ligase binding [GO:0031625]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
|
PTM: Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. {ECO:0000269|PubMed:21118996}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21118996, ECO:0000269|PubMed:9448268}. Cytoplasm {ECO:0000269|PubMed:21118996}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000269|PubMed:21118996}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:17785444}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:17785444};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination (PubMed:10391247, PubMed:11745377, PubMed:12482967, PubMed:12556497, PubMed:14720327, PubMed:15004007, PubMed:17785444, PubMed:18765672, PubMed:20874444, PubMed:21118996, PubMed:9448268). Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2 (PubMed:15004007). Negative regulator of the canonical Wnt/beta-catenin signaling pathway (PubMed:20194509). Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1 (PubMed:12556497). Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes (PubMed:12556497). Negative regulator of the Notch signaling pathway (PubMed:20118921). Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1 (PubMed:20118921). Negative regulator of the MYB family of transcription factors (PubMed:16055500). Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP (PubMed:15082531, PubMed:15308626, PubMed:16055500). Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself (PubMed:15082531, PubMed:15308626, PubMed:16055500). Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1 (PubMed:15004007). Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members (By similarity). Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner (By similarity). Acts as an inhibitor of the mTORC1 complex in response to osmotic stress by mediating phosphorylation of RPTOR, thereby preventing recruitment of the mTORC1 complex to lysosomes (By similarity). {ECO:0000250|UniProtKB:Q9UBE8, ECO:0000269|PubMed:10391247, ECO:0000269|PubMed:11745377, ECO:0000269|PubMed:12482967, ECO:0000269|PubMed:12556497, ECO:0000269|PubMed:14720327, ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15308626, ECO:0000269|PubMed:16055500, ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:18765672, ECO:0000269|PubMed:20118921, ECO:0000269|PubMed:20194509, ECO:0000269|PubMed:20874444, ECO:0000269|PubMed:21118996, ECO:0000269|PubMed:9448268}.
|
Mus musculus (Mouse)
|
O54950
|
AAKG1_MOUSE
|
MESVAAESSPALENEHFQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLQELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQALVLTGGEKKP
| null | null |
cellular response to nutrient levels [GO:0031669]; fatty acid biosynthetic process [GO:0006633]; import into nucleus [GO:0051170]; positive regulation of gene expression [GO:0010628]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleotide-activated protein kinase complex [GO:0031588]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
ADP binding [GO:0043531]; AMP binding [GO:0016208]; AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887]; protein-containing complex binding [GO:0044877]
|
PF00571;
|
3.10.580.10;
|
5'-AMP-activated protein kinase gamma subunit family
|
PTM: Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. {ECO:0000269|PubMed:21460634}.; PTM: Glycosylated; O-GlcNAcylated by OGT, promoting the AMP-activated protein kinase (AMPK) activity. {ECO:0000250|UniProtKB:P54619}.
| null | null | null | null | null | null |
FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. {ECO:0000250|UniProtKB:P54619}.
|
Mus musculus (Mouse)
|
O54951
|
SEM6B_MOUSE
|
MWTPRVPPPRPALSFFLLLLLGVTYGLFPEEPPPLSVAPRDYLSHYPVFVGSGPGRLTAAEGAEDLNIQRVLRVNRTLFIGDRDNLYQVELEPSTSTELRYQRKLTWRSNPSDIDVCRMKGKQEGECRNFVKVLLLRDESTLFVCGSNAFNPICANYSMDTLQLLGDSISGMARCPYDPKHANVALFSDGMLFTATVTDFLAIDAVIYRSLGDRPTLRTVKHDSKWFKEPYFVHAVEWGSHVYFFFREIAMEFNYLEKVVVSRVARVCKNDVGGSPRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVTGVVSLGGRPVILAVFSTPSNSIPGSAVCAFDMNQVAAVFEGRFREQKSPESIWTPVPEDQVPRPRPGCCAAPGMQYNASSALPDEILNFVKTHPLMDEAVPSLGHSPWIVRTLMRHQLTRVAVDVGAGPWGNQTIVFLGSEAGTVLKFLVKPNASVSGTTGPSIFLEEFETYRPDRCGRPSSAGEWGQRLLSLELDAASGGLLAAFPRCVVRVPVARCQLYSGCMKNCIGSQDPYCGWAPDGSCIFLRPGTSATFEQDVSGASTSGLGDCTGLLRASLSDDRAGLVSVNLLVTSSVAAFVVGAVVSGFSVGWFVGLRERRELARRKDKEAILAHGGSEAVLSVSRLGERRGTGPGGRGGAGGGPGGPPEALLAPLMQNGWTKAALLHGGPHDLDTGLLPTPEQTPLPQKRLPTPHPHAHALGSRAWDHSHALLSASASTSLLLLAPARASEQPQVPAEPGPESRLCAPRSCRASHPGDFPLTPHASPDRRRVVSAPTGPLDPSVGDGLPGPWSPPATSSLRRPGPHGPPTAALRRTHTFNSGEARPGGHRPRRHPPADSTHLLPCGTGERTAPPVP
| null | null |
axon guidance [GO:0007411]; central nervous system development [GO:0007417]; hippocampus development [GO:0021766]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; neural crest cell migration [GO:0001755]; positive regulation of cell migration [GO:0030335]; semaphorin-plexin signaling pathway [GO:0071526]
|
plasma membrane [GO:0005886]
|
chemorepellent activity [GO:0045499]; semaphorin receptor binding [GO:0030215]
|
PF01437;PF01403;
|
3.30.1680.10;2.130.10.10;
|
Semaphorin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:20484647}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Functions as a cell surface repellent for mossy fibers of developing neurons in the hippocampus where it plays a role in axon guidance (PubMed:20484647). May function through the PLXNA4 receptor expressed by mossy cell axons (PubMed:20484647). {ECO:0000269|PubMed:20484647}.
|
Mus musculus (Mouse)
|
O54952
|
BRCA1_RAT
|
MDLSAVRIQEVQNVLHAMQKILECPICLELIKEPVSTQCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVEELLKIIDAFELDTGMQCANGFSFSKKKNSSSELLNEDASIIQSVGYRNRVKKLQQIESGSATLKDSLSVQLSNLGIVRSMKKNRQTQPQNKSVYIALESDSSEERVNAPDGCSVRDQELFQIAPGGAGDEGKLNSAKKAACDFSEGIRNIEHHQCSDKDLNPTENHATERHPEKCPRISVANVHVEPCGTDARASSLQRGTRSLLFTEDRLDAEKAEFCDRSKQSGAAVSQQSRWADSKETCNGRPVPRTEGKADPNVDSLCGRKQWNHPKSLCPENSGATTDVPWITLNSSIQKVNEWFSRTGEMLTSDNASDRRPASNAEAAVVLEVSNEVDGCFSSSKKIDLVAPDPDNAVMCTSGRDFSKPVENIINDKIFGKTYQRKGSRPHLNHVTEIIGTFTTEPQIIQEQPFTNKLKRKRSTCLHPEDFIKKADLTVVQRISENLNQGTDQMEPNDQAMSITSNGQENRATGNDLQRGRNAHPIESLRKEPAFTAKAKSISNSISDLEVELNVHSSKAPKKNRLRRKSTRCVLPLEPISRNPSPPTCAELQIESCGSSEETKKNNSNQTPAGHIREPQLIEDTEPAADAKKNEPNEHIRKRSASDAFPEEKLMNKAGLLTSCSSPRKPQGPVNPSPERKGIEQLEMCQMPDNNKELGDLVLGGEPSGKPTEPSEESTSVSLVPDTDYDTQNSVSILEANTVRYARTGSVQCMTQFVASENPKELVHGSNNAGSGSECFKHPLRHELNHNQETIEMEDSELDTQYLQNTFQVSKRQSFALFSKLRSPQKDCTLVGARSVPSREPSPKVTSRGEQKERQGQEESEISHVQAVTVTVGLPVPCQEGKPGAVTMCADVSRLCPSSHYRSCENGLNTTDKSGISQNSHFRQSVSPLRSSIKTDNRKTLTEGRFEKHTERGMGNETAVQSTIHTISLNNRGDACLEASSGSVIEVHSTGENVQGQLDRNRGPKVNTVSLLDSTQPGVSKQSAPVSDKYLEIKQESKAVSADFSPCLFSDHLEKPMRSDKTFQVCSETPDDLLDDVEIQENASFGEGGITEKSAIFNGSVLRRESSRSPSPVTHASKSRSLHRGSRKLEFSEESDSTEDEDLPCFQHLLSRVSSTPELTRCSSVVTQRVPEKAKGTQAPRKSSISDCNNEVILGEASQEYQFSEDAKCSGSMFSSQHSAALGSPANALSQDPDFNPPSKQRRHQAENEEAFLSDKELISDHEDMAACLEEASDQEEDSIIPDSVASGYESEANLSEDCSQSDILTTQQRATMKDNLIKLQQEMAQLEAVLEQHGSQPSGHPPCLPADPCALEDLPDPEQNRSGTAILTSKNINENPVSQNPKRACDDKSQPQPPDGLPSGDKESGMRRPSPFKSPLTSSRCSARGHSRSLQNRNSTSQEELLQPAXLEKSCEPHNLTGRSCLPRQDLEGTPYPESGIRLVSSRDPDSESPKVSALVCTAPASTSALKISQGQVAGSCRSPAAGGADTAVVEIVSKIKPEVTSPKERAERDISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVIKSIQERKLLSVHEFEVKGDVVTGSNHQGPRRSRESQEKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDTGAHPIVLVQPSAWTEDNDCPDIGQLCKGRLVMWDWVLDSISVYRCRDLDAYLVQNITCGRDGSEPQDSND
|
2.3.2.27
| null |
cellular response to indole-3-methanol [GO:0071681]; cellular response to ionizing radiation [GO:0071479]; cellular response to tumor necrosis factor [GO:0071356]; centrosome cycle [GO:0007098]; chordate embryonic development [GO:0043009]; chromosome segregation [GO:0007059]; DNA damage response [GO:0006974]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; fatty acid biosynthetic process [GO:0006633]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; localization [GO:0051179]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; mitotic G2/M transition checkpoint [GO:0044818]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of fatty acid biosynthetic process [GO:0045717]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of angiogenesis [GO:0045766]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular endothelial growth factor production [GO:0010575]; postreplication repair [GO:0006301]; protein autoubiquitination [GO:0051865]; protein K6-linked ubiquitination [GO:0085020]; protein ubiquitination [GO:0016567]; random inactivation of X chromosome [GO:0060816]; regulation of cell cycle [GO:0051726]; regulation of transcription by RNA polymerase II [GO:0006357]; response to estradiol [GO:0032355]; response to ionizing radiation [GO:0010212]; response to lipid [GO:0033993]; response to nutrient [GO:0007584]; response to organic substance [GO:0010033]; sex-chromosome dosage compensation [GO:0007549]
|
BRCA1-A complex [GO:0070531]; BRCA1-B complex [GO:0070532]; BRCA1-BARD1 complex [GO:0031436]; BRCA1-C complex [GO:0070533]; chromosome [GO:0005694]; condensed chromosome [GO:0000793]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; DNA repair complex [GO:1990391]; intracellular non-membrane-bounded organelle [GO:0043232]; lateral element [GO:0000800]; male germ cell nucleus [GO:0001673]; mitochondrial matrix [GO:0005759]; nuclear ubiquitin ligase complex [GO:0000152]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; ribonucleoprotein complex [GO:1990904]; XY body [GO:0001741]
|
chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA-binding transcription activator activity [GO:0001216]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; p53 binding [GO:0002039]; RNA binding [GO:0003723]; RNA polymerase binding [GO:0070063]; transcription cis-regulatory region binding [GO:0000976]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF00533;PF12820;PF00097;
|
3.40.50.10190;3.30.40.10;
| null |
PTM: Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Phosphorylation at Ser-975 by CHEK2 regulates mitotic spindle assembly. Phosphorylation by AURKA regulates centrosomal microtubule nucleation. {ECO:0000250|UniProtKB:P38398}.; PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation. {ECO:0000250|UniProtKB:P38398}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}. Chromosome {ECO:0000250|UniProtKB:P48754}. Cytoplasm {ECO:0000250|UniProtKB:P38398}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. Translocated to the cytoplasm during UV-induced apoptosis. {ECO:0000250|UniProtKB:P38398}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P38398};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Required for FANCD2 targeting to sites of DNA damage. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator. {ECO:0000250|UniProtKB:P38398}.
|
Rattus norvegicus (Rat)
|
O54957
|
LAT_MOUSE
|
MEADALSPVGLGLLLLPFLVTLLAALCVRCRELPVSYDSTSTESLYPRSILIKPPQITVPRTPAVSYPLVTSFPPLRQPDLLPIPRSPQPLGGSHRMPSSQQNSDDANSVASYENQEPACKNVDADEDEDDYPNGYLVVLPDSSPAAVPVVSSAPVPSNPDLGDSAFSVESCEDYVNVPESEESAEASLDGSREYVNVSPEQQPVTRAELASVNSQEVEDEGEEEGVDGEEAPDYENLQELN
| null | null |
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; cellular defense response [GO:0006968]; gene expression [GO:0010467]; homeostasis of number of cells [GO:0048872]; immune response [GO:0006955]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; lymphocyte homeostasis [GO:0002260]; mast cell degranulation [GO:0043303]; Ras protein signal transduction [GO:0007265]; regulation of T cell activation [GO:0050863]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cell-cell junction [GO:0005911]; COP9 signalosome [GO:0008180]; Golgi apparatus [GO:0005794]; immunological synapse [GO:0001772]; plasma membrane [GO:0005886]
|
protein kinase binding [GO:0019901]; signaling receptor complex adaptor activity [GO:0030159]
|
PF15234;
| null | null |
PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ. Phosphorylated by ITK leading to the recruitment of VAV1 to LAT-containing complexes (By similarity). {ECO:0000250}.; PTM: Palmitoylation of Cys-27 and Cys-30 is required for raft targeting and efficient phosphorylation. {ECO:0000250}.; PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ. Phosphorylated by ITK leading to the recruitment of VAV1 to LAT-containing complexes. {ECO:0000250|UniProtKB:O43561}.; PTM: 'Lys-63'-linked ubiquitinated by TRAF6. {ECO:0000250|UniProtKB:O43561}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein. Note=Present in lipid rafts.
| null | null | null | null | null |
FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules. {ECO:0000269|PubMed:10843385}.
|
Mus musculus (Mouse)
|
O54960
|
CAPON_RAT
|
MPSKTKYNLVDDGHDLRIPLHNEDAFQHGISFEAKYVGSLDVPRPNSRVEIVAAMRRIRYEFKAKNIKKKKVSIMVSVDGVKVILKKKKKKKEWTWDESKMLVMQDPIYRIFYVSHDSQDLKIFSYIARDGASNIFRCNVFKSKKKSQAMRIVRTVGQAFEVCHKLSLQHTQQNADGQEDGESERNSDGSGDPGRQLTGAERVSTATAEETDIDAVEVPLPGNDILEFSRGVTDLDAIGKDGGSHIDTTVSPHPQEPMLAASPRMLLPSSSSSKPPGLGTGTPLSTHHQMQLLQQLLQQQQQQTQVAVAQVHLLKDQLAAEAAARLEAQARVHQLLLQNKDMLQHISLLVKQVQELELKLSGQSTMGSQDSLLEITFRSGALPVLCESTTPKPEDLHSPLLGAGLADFAHPVGSPLGRRDCLVKLECFRFLPAEDNQPMAQGEPLLGGLELIKFRESGIASEYESNTDESEERDSWSQEELPRLLNVLQRQELGDSLDDEIAV
| null | null |
neuron projection regeneration [GO:0031102]; neurotransmitter secretion [GO:0007269]; positive regulation of peptidyl-cysteine S-nitrosylation [GO:2000170]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1902514]; regulation of cardiac muscle cell action potential [GO:0098901]; regulation of heart rate by chemical signal [GO:0003062]; regulation of high voltage-gated calcium channel activity [GO:1901841]; regulation of nitric oxide biosynthetic process [GO:0045428]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]
|
anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; podosome [GO:0002102]; postsynapse [GO:0098794]; presynapse [GO:0098793]; sarcoplasmic reticulum membrane [GO:0033017]; Z disc [GO:0030018]
|
mitogen-activated protein kinase kinase binding [GO:0031434]; nitric-oxide synthase binding [GO:0050998]; PDZ domain binding [GO:0030165]; protease binding [GO:0002020]; signaling adaptor activity [GO:0035591]
|
PF00640;
|
2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000269|PubMed:33523862}. Cell projection, podosome {ECO:0000269|PubMed:33523862}.
| null | null | null | null | null |
FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4. In kidney podocytes, plays a role in podosomes and filopodia formation through CDC42 activation (PubMed:33523862). {ECO:0000269|PubMed:33523862, ECO:0000269|PubMed:9459447}.
|
Rattus norvegicus (Rat)
|
O54962
|
BAF_MOUSE
|
MTTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL
| null | null |
chromatin organization [GO:0006325]; chromosome organization [GO:0051276]; DNA integration [GO:0015074]; establishment of integrated proviral latency [GO:0075713]; mitotic nuclear membrane reassembly [GO:0007084]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of innate immune response [GO:0045824]; negative regulation of protein ADP-ribosylation [GO:0010836]; negative regulation of type I interferon production [GO:0032480]; negative regulation of viral genome replication [GO:0045071]; response to oxidative stress [GO:0006979]
|
chromatin [GO:0000785]; condensed chromosome [GO:0000793]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF02961;
|
1.10.150.40;
|
BAF family
|
PTM: Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins. Non phosphorylated BAF seems to enhance binding between EMD and LMNA. Dephosphorylated by protein phosphatase 2A (PP2A) following interaction with ANKLE2/LEM4 during mitotic exit, leading to mitotic nuclear envelope reassembly. {ECO:0000250|UniProtKB:O75531}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. {ECO:0000250|UniProtKB:O75531}.
| null | null | null | null | null |
FUNCTION: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (By similarity). Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (By similarity). Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner (By similarity). Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface (By similarity). Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity (PubMed:32156810). Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (By similarity). Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (By similarity). Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy (By similarity). {ECO:0000250|UniProtKB:O75531, ECO:0000269|PubMed:32156810}.
|
Mus musculus (Mouse)
|
O54963
|
REST_RAT
|
MATQVMGQSSGGGSLFNNSGNMGMALPNDMYDLHDLSKAELAAPQLIMLANVALTGEVNGSCCDYLVGEERQMAELMPVGDNHFSDSEGEGLEESAELKGDPSGLDNMELRSLELSVVEPQPVFEASAAPEVYSSNKDPAPEAPVAEDKCKNLKAKPFRCKPCQYEAESEEQFVHHIRVHSAKKFFVEESAEKQAKARESGASPSEEGEFSKGPIRCDRCGYNTNRYDHYTAHLKHHLRAGDNERVYKCIICTYTTVSEYHWRKHLRNHFPRKVYTCSKCNYFSTEKNNYVQHVRTHTGERPYKCELCPYSSSQKTHLTRHMRTHSGEKPFKCDQCNYVASNQHEVTRHARQVHNGPKPLNCPHCDYKTADRSNFKKHVELHVNPRQFNCPVCDYAASKKCNLQYHFKSKHPTCPSKTMDVSKVKLKKTKRREADLHRDAAAAATEQTDTEQAKTKGVDASARRSERPVKGVGKDVPKEKKPCSNASVVQVTTRTRKSAVETKAAEGKHTDGQTGNNAEKSSKAKKSKRKMDAEAHPSVEPVTEGPVTKKKKTESKPKTSGEVPKGSRVEDRKADKQQSASIKKGGKKTALKTKTAKKGSKLAPKWVGHTEPSSEMAQGGESPVPALTQAVVTPSGSTQTELSSPMDIAQTEPAQMDVSQTGPPQVQRPLPVEPAQLEPSPPQEPPQVEPPACVEPPPPVEPPCPMEPAEMEPSPPMEPSQVEPPPHLEPPLPMELPQVELPPVEDCQKELPPVEHAQTKVAQTGPTQVGAVQEEPLFCLRATSSQANQKVISPKDRAKEKLSVLSEMARQEQVLIEVGLVPVRDSQLLKASKSAPDLPAPPSPLPKGHLRREETPKDQEMFSDGEGNKVSPLEKGGTEEAGESRAELAAPMESTSALSSEQSSNAPDGETLHSECQADSTAVCEMEVDTEQKTDRVPLKDSAVEPVSPLNPRVDPEAAAPAVVASPPITLAESQEIDEDEGIHSHDGSDLSDNMSEGSDDSGLHGARPAPQEATSKSGKEGLAVKVTEGEFVCIFCDRSFRKEKDYSKHLNRHLVNVYFLEEAAEEQE
| null | null |
auditory receptor cell stereocilium organization [GO:0060088]; cardiac muscle cell myoblast differentiation [GO:0060379]; cellular response to electrical stimulus [GO:0071257]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to xenobiotic stimulus [GO:0071466]; chromatin remodeling [GO:0006338]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; hematopoietic progenitor cell differentiation [GO:0002244]; modification of synaptic structure [GO:0099563]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of aldosterone biosynthetic process [GO:0032348]; negative regulation of amniotic stem cell differentiation [GO:2000798]; negative regulation of calcium ion-dependent exocytosis [GO:0045955]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cortisol biosynthetic process [GO:2000065]; negative regulation of dense core granule biogenesis [GO:2000706]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of insulin secretion [GO:0046676]; negative regulation of mesenchymal stem cell differentiation [GO:2000740]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of neurogenesis [GO:0050768]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription regulatory region DNA binding [GO:2000678]; nervous system process [GO:0050877]; neuromuscular process controlling balance [GO:0050885]; neuron differentiation [GO:0030182]; neuronal stem cell population maintenance [GO:0097150]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of programmed cell death [GO:0043068]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; regulation of osteoblast differentiation [GO:0045667]; response to hypoxia [GO:0001666]; response to ischemia [GO:0002931]; somatic stem cell population maintenance [GO:0035019]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription repressor complex [GO:0017053]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
PF00096;
|
3.30.160.60;
| null |
PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q8VIG1}.; PTM: Phosphorylated; phosphorylation is required for ubiquitination. {ECO:0000250|UniProtKB:Q13127}.; PTM: Ubiquitinated; ubiquitination is mediated by BTRC and leads to proteasomal degradation in G2 phase (By similarity). Ubiquitination increases during neuronal differentiation (By similarity). Deubiquitinated by USP7; leading to its stabilization and promoting the maintenance of neural progenitor cells (By similarity). {ECO:0000250|UniProtKB:Q13127}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10490617, ECO:0000269|PubMed:12657670, ECO:0000269|PubMed:22371606, ECO:0000269|PubMed:22960932}. Cytoplasm {ECO:0000250|UniProtKB:Q13127}. Note=Colocalizes with ZFP90 in the nucleus (By similarity). In response to hypoxia, there is a more pronounced increase in levels in the nucleus as compared to the cytoplasm (By similarity). In aging neurons, increased levels in the nucleus as compared to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q13127, ECO:0000250|UniProtKB:Q8VIG1}.; SUBCELLULAR LOCATION: [Isoform 6]: Nucleus {ECO:0000250|UniProtKB:Q13127}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells (By similarity). Restricts the expression of neuronal genes by associating with two distinct corepressors, SIN3A and RCOR1, which in turn recruit histone deacetylase to the promoters of REST-regulated genes (By similarity). Mediates repression by recruiting the BHC complex at RE1/NRSE sites which acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier (PubMed:9454838). Transcriptional repression by REST-CDYL via the recruitment of histone methyltransferase EHMT2 may be important in transformation suppression (By similarity). Represses the expression of SRRM4 in non-neural cells to prevent the activation of neural-specific splicing events and to prevent production of REST isoform 6 (By similarity). Repressor activity may be inhibited by forming heterodimers with isoform 6, thereby preventing binding to NRSE or binding to corepressors and leading to derepression of target genes (By similarity). Also maintains repression of neuronal genes in neural stem cells, and allows transcription and differentiation into neurons by dissociation from RE1/NRSE sites of target genes (By similarity). Thereby is involved in maintaining the quiescent state of adult hippocampal neural stem cells and preventing premature differentiation into mature neurons (By similarity). Plays a role in the developmental switch in synaptic NMDA receptor composition during postnatal development, by repressing GRIN2B expression and thereby altering NMDA receptor properties from containing primarily GRIN2B to primarily GRIN2A subunits (PubMed:22960932). Acts as a regulator of osteoblast differentiation (By similarity). Key repressor of gene expression in hypoxia; represses genes in hypoxia by direct binding to an RE1/NRSE site on their promoter regions (By similarity). May also function in stress resistance in the brain during aging; possibly by regulating expression of genes involved in cell death and in the stress response (By similarity). Repressor of gene expression in the hippocampus after ischemia by directly binding to RE1/NRSE sites and recruiting SIN3A and RCOR1 to promoters of target genes, thereby promoting changes in chromatin modifications and ischemia-induced cell death (PubMed:12657670, PubMed:22371606). After ischemia, might play a role in repression of miR-132 expression in hippocampal neurons, thereby leading to neuronal cell death (PubMed:25108103). {ECO:0000250|UniProtKB:Q13127, ECO:0000250|UniProtKB:Q8VIG1, ECO:0000269|PubMed:12657670, ECO:0000269|PubMed:22371606, ECO:0000269|PubMed:22960932, ECO:0000269|PubMed:25108103, ECO:0000269|PubMed:9454838}.; FUNCTION: [Isoform 6]: Binds to the 3' region of the neuron-restrictive silencer element (NRSE), with lower affinity than full-length REST isoform 1 (By similarity). Exhibits weaker repressor activity compared to isoform 1 (By similarity). May negatively regulate the repressor activity of isoform 1 by binding to isoform 1, thereby preventing its binding to NRSE and leading to derepression of target genes (By similarity). However, in another study, does not appear to be implicated in repressor activity of a NRSE motif-containing reporter construct nor in inhibitory activity on the isoform 1 transcriptional repressor activity (By similarity). Post-transcriptional inactivation of REST by SRRM4-dependent alternative splicing into isoform 6 is required in mechanosensory hair cells in the inner ear for derepression of neuronal genes and hearing (By similarity). {ECO:0000250|UniProtKB:Q13127, ECO:0000250|UniProtKB:Q8VIG1}.
|
Rattus norvegicus (Rat)
|
O54965
|
RNF13_MOUSE
|
MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFEDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPLKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIDTLKKIDIPSVFIGESSANSLKDEFTYEKGGHIILVPELSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRNRRNRLRKDQLKKLPVHKFKKGDEYDVCAICLEEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENQVSEHTPLLPPSASARTQSFGSLSESHSHHNMTESSDYEDDDNEETDSSDADNEITDHSVVVQLQPNGEQDYNIANTV
|
2.3.2.27
| null |
organelle localization [GO:0051640]; positive regulation of JNK cascade [GO:0046330]; protein autoubiquitination [GO:0051865]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; nuclear inner membrane [GO:0005637]; nucleoplasm [GO:0005654]
|
JUN kinase binding [GO:0008432]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF02225;PF13639;
|
3.50.30.30;3.30.40.10;
| null |
PTM: Autoubiquitinated. {ECO:0000269|PubMed:19292867}.; PTM: N-glycosylated and also modified with chondroitin sulfate. {ECO:0000269|PubMed:19292867}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:19292867}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19292867}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:20230530}; Single-pass type I membrane protein {ECO:0000255}. Note=The mature protein is subjected to extensive proteolysis that leads to the shedding of the ectodomain into the lumen of vesicles and the release of the C-terminal fragment into the cytosol (PubMed:20230530). Not detected in early endosomes (PubMed:20230530). Treatment of the cells with either PMA or ionomycin stabilizes the full-length protein which relocalizes to recycling endosomes and to the inner nuclear membrane (PubMed:20230530). {ECO:0000269|PubMed:20230530}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:19292867};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:19292867}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that regulates cell proliferation (PubMed:19292867). Involved in apoptosis regulation (By similarity). Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (By similarity). Also involved in protein trafficking and localization (By similarity). {ECO:0000250|UniProtKB:O43567, ECO:0000269|PubMed:19292867}.
|
Mus musculus (Mouse)
|
O54967
|
ACK1_MOUSE
|
MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNITRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKAMCKRKSWMSKVFSGKRLEAEFPSQHSQSTFRKPSPTPGSLPGEGTLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPAGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTLPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMAYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPTQHLGRVKREPPPRPPQPAIFTQKTTYDPVSEDPDPLSSDFKRLGLRKPALPRGLWLAKPSARVPGTKADRSSGGEVTLIDFGEEPVVPTPRPCAPSLAQLAMDACSLLDKTPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEVCSINSTLVGAGLPAGPSQGETNYAFVPEQAQMPPALEDNLFLPPQGGGKPPSSVQTAEIFQALQQECMRQLQVPTGQLTPSPTPGGDDKPQVPPRVPIPPRPTRPRVELSPAPSGEEETSRWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPHRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGRKVSSTHYYLLPERPPYLERYQRFLREAQSPEEPAALPVPPLLPPPSTPAPAAPTATVRPMPQAAPDPKANFSTNNSNPGARPPSLRAAARLPQRGCPGDGQEAARPADKVQMLQAMVHGVTTEECQAALQSHSWSVQRAAQYLKVEQLFGLGLRPRVECHKVLEMFDWNLEQAGCHLLGSCGPAHHKR
|
2.7.10.2; 2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
endocytosis [GO:0006897]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; phosphorylation [GO:0016310]; regulation of keratinocyte differentiation [GO:0045616]; signal transduction [GO:0007165]; spermatid development [GO:0007286]
|
adherens junction [GO:0005912]; axon [GO:0030424]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]; WW domain binding [GO:0050699]
|
PF09027;PF11555;PF07714;PF14604;
|
4.10.680.10;1.10.8.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family
|
PTM: Autophosphorylation regulates kinase activity. Phosphorylation on Tyr-533 is required for interaction with SRC and is observed during association with clathrin-coated pits (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent. {ECO:0000269|PubMed:20086093}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16777958, ECO:0000269|PubMed:20333297}. Nucleus {ECO:0000269|PubMed:20333297}. Endosome {ECO:0000269|PubMed:17182860}. Cell junction, adherens junction {ECO:0000269|PubMed:18477472}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q07912}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q07912}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:21169560}. Cytoplasm, cytosol {ECO:0000269|PubMed:25223282}. Note=The Tyr-284 phosphorylated form is found both in the membrane and nucleus (PubMed:20333297). Co-localizes with EGFR on endosomes (PubMed:17182860). Nuclear translocation is CDC42-dependent (PubMed:21169560). Detected in long filamentous cytosolic structures where it co-localizes with CTPS1 (PubMed:25223282). {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:21169560, ECO:0000269|PubMed:25223282}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR. {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20333297}.
|
Mus musculus (Mouse)
|
O54968
|
NF2L2_RAT
|
MMDLELPPPGLQSQQDMDLIDILWRQDIDLGVSREVFDFSQRQKDYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQTDTSGSVSYSQVAHIPKQDALYFEDCMQLLAETFPFVDDHEVSSPTFQSLALDIPSHVESSVFTTPDQAQSLDSSLETAMTDLSSIQQDMEQVWQELFSIPELQCLNTENKQQAETTTVPSPEATLTEMDSNYHFYSSIPSLEKEVDSCSPHFLHGFEDSFSSILSTDDASQLNSLDSNPTLNTDFGDEFYSAFLAEPSGGGSMPSSAAISQSLSELLGGPIEGCDLSLCKAFNQKHTEGTVEFNDSDSGISLNTSPSRASPEHSVESSIYGDPPPGFSDSEMEELDSAPGSVKQNGPKAQPTHSSGDTVQPLSPAQGHSAAVHESQCENTTKKEVPVSPGHQKVPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVDDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLGHLKDEREKLLREKGENDRNLHLLKRKLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDTKKN
| null | null |
aflatoxin catabolic process [GO:0046223]; cell redox homeostasis [GO:0045454]; cellular response to angiotensin [GO:1904385]; cellular response to copper ion [GO:0071280]; cellular response to fluid shear stress [GO:0071498]; cellular response to glucose starvation [GO:0042149]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to oxidative stress [GO:0034599]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to xenobiotic stimulus [GO:0071466]; endoplasmic reticulum unfolded protein response [GO:0030968]; inflammatory response [GO:0006954]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of cellular response to hypoxia [GO:1900038]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of hematopoietic stem cell differentiation [GO:1902037]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of vascular associated smooth muscle cell migration [GO:1904753]; PERK-mediated unfolded protein response [GO:0036499]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood coagulation [GO:0030194]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose import [GO:0046326]; positive regulation of glutathione biosynthetic process [GO:1903788]; positive regulation of neuron projection development [GO:0010976]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; regulation of cellular response to oxidative stress [GO:1900407]; regulation of DNA-templated transcription [GO:0006355]; regulation of embryonic development [GO:0045995]; regulation of innate immune response [GO:0045088]; regulation of removal of superoxide radicals [GO:2000121]; regulation of transcription by RNA polymerase II [GO:0006357]; response to endoplasmic reticulum stress [GO:0034976]; response to ischemia [GO:0002931]; response to organic substance [GO:0010033]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410]
|
centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-DNA complex [GO:0032993]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; molecular condensate scaffold activity [GO:0140693]; protein domain specific binding [GO:0019904]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator binding [GO:0001221]; ubiquitin protein ligase binding [GO:0031625]
|
PF03131;
|
1.10.880.10;
|
BZIP family, CNC subfamily
|
PTM: Ubiquitinated in the cytoplasm by the BCR(KEAP1) E3 ubiquitin ligase complex leading to its degradation. In response to oxidative stress, electrophile metabolites, such as sulforaphane, modify KEAP1, leading to inhibit activity of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and activity. In response to autophagy, the BCR(KEAP1) complex is inactivated. {ECO:0000250|UniProtKB:Q60795}.; PTM: Phosphorylation of Ser-40 by PKC in response to oxidative stress dissociates NFE2L2 from its cytoplasmic inhibitor KEAP1, promoting its translocation into the nucleus. {ECO:0000269|PubMed:12198130}.; PTM: Acetylation at Lys-595 and Lys-598 increases nuclear localization whereas deacetylation by SIRT1 enhances cytoplasmic presence. {ECO:0000250|UniProtKB:Q16236}.; PTM: Glycation impairs transcription factor activity by preventing heterodimerization with small Maf proteins. Deglycation by FN3K restores activity. {ECO:0000250|UniProtKB:Q16236}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q60795}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:16314513}. Note=Cytosolic under unstressed conditions: ubiquitinated and degraded by the BCR(KEAP1) E3 ubiquitin ligase complex. Translocates into the nucleus upon induction by electrophilic agents that inactivate the BCR(KEAP1) E3 ubiquitin ligase complex. {ECO:0000250|UniProtKB:Q60795}.
| null | null | null | null | null |
FUNCTION: Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles (PubMed:16314513). In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex. In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the small Maf proteins and binding to ARE elements of cytoprotective target genes. The NFE2L2/NRF2 pathway is also activated in response to selective autophagy: autophagy promotes interaction between KEAP1 and SQSTM1/p62 and subsequent inactivation of the BCR(KEAP1) complex, leading to NFE2L2/NRF2 nuclear accumulation and expression of cytoprotective genes (By similarity). May also be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region (By similarity). Also plays an important role in the regulation of the innate immune response. It is a critical regulator of the innate immune response and survival during sepsis by maintaining redox homeostasis and restraint of the dysregulation of pro-inflammatory signaling pathways like MyD88-dependent and -independent and TNF-alpha signaling. Suppresses macrophage inflammatory response by blocking pro-inflammatory cytokine transcription and the induction of IL6. Binds to the proximity of pro-inflammatory genes in macrophages and inhibits RNA Pol II recruitment. The inhibition is independent of the Nrf2-binding motif and reactive oxygen species level (By similarity). Represses antiviral cytosolic DNA sensing by suppressing the expression of the adapter protein STING1 and decreasing responsiveness to STING1 agonists while increasing susceptibility to infection with DNA viruses (By similarity). {ECO:0000250|UniProtKB:Q16236, ECO:0000250|UniProtKB:Q60795, ECO:0000269|PubMed:16314513}.
|
Rattus norvegicus (Rat)
|
O54972
|
MTG16_MOUSE
|
MSQASTTTLESGALLSGPRGLQYGSPAHRKEKAAAMPDSPAEVKTQPRSTPPSMPPPPPTSSQGATRPPSFTPHTHGEDGPATSLPHGRFHGCLKWSMVCLLMNGSSHSPTAIHGAPSTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHAKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQTPAQYLAQHEQLLLDASATSPVDSSELLLEVNENGKRRTPDRTKENGSDRDPLHPDHLSKRSCTLSPAQRCSPSNGLPHPTPPPPPHYRLEDMAMAHHFRDSYRHPDPRELRERHRPLAIPGSRQEEVIDHRLTEREWAEEWKHLNSLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWIRCYSDSEEGKKGPTPISARSLNSCSGPEGSQLDVHRDFTPRTLSGYMPEEIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKMERALAEAKRQASEDALTVINQQEDSSESCWNCGRKASETCSGCNAARYCGSFCQHKDWEKHHHVCGQSLQGPAAAVADPLPGQPDATASPSEAGSAGPSRPCSPGPPGPLDAAVPR
| null | null |
DNA-templated transcription [GO:0006351]; granulocyte differentiation [GO:0030851]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of glycolytic process [GO:0045820]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of aerobic respiration [GO:1903715]; response to hypoxia [GO:0001666]
|
Golgi membrane [GO:0000139]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]
|
PF08788;PF07531;PF01753;
|
6.10.140.2220;6.10.250.230;1.20.120.1110;
|
CBFA2T family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10022820}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10022820}. Golgi apparatus membrane {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Can repress the expression of MMP7 in a ZBTB33-dependent manner. Reduces the protein levels and stability of the transcriptinal regulator HIF1A; interacts with EGLN1 and promotes the HIF1A prolyl hydroxylation-dependent ubiquitination and proteasomal degradation pathway. Contributes to inhibition of glycolysis and stimulation of mitochondrial respiration by down-regulating the expression of glycolytic genes including PFKFB3, PFKFB4, PDK1, PFKP, LDHA and HK1 which are direct targets of HIF1A (By similarity). Regulates the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (PubMed:16407974). Plays a role in granulocyte differentiation (PubMed:15231665). {ECO:0000250|UniProtKB:O75081, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:15231665, ECO:0000269|PubMed:16407974}.
|
Mus musculus (Mouse)
|
O54975
|
XPP1_RAT
|
MAPKVTSELLRQLRQAMRNSECVAEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDNNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLVPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLFIDGDRIDAPGVKQHLLLDLGLEAEYKIQVLPYKSILSELKTLCADLSPREKVWVSDKASYAVSEAIPKDHRCCMPYTPICIAKAVKNSAESAGMRRAHIKDAVALCELFNWLEQEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGRQEALEWLLRETEPISRQH
|
3.4.11.9
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NQW7}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:Q9NQW7};
|
bradykinin catabolic process [GO:0010815]; negative regulation of programmed cell death [GO:0043069]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
aminopeptidase activity [GO:0004177]; manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; protein homodimerization activity [GO:0042803]
|
PF01321;PF16189;PF00557;PF16188;
|
3.90.230.10;3.40.350.10;
|
Peptidase M24B family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10095056}.
|
CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:10095056};
| null | null | null | null |
FUNCTION: Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (PubMed:10095056). Contributes to the degradation of bradykinin (By similarity). {ECO:0000250|UniProtKB:Q9NQW7, ECO:0000269|PubMed:10095056}.
|
Rattus norvegicus (Rat)
|
O54980
|
SNG2_RAT
|
MESGAYGAANAGGSFDLRRYVSQPQVVTRLVSMVLALIVFSCIFGEGYINLHSSDQLHCVFNRNEDACRYGSAIGVLAFLASAFFLVVDAFFSQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAATKPDDVLVGADSARAAITFSFFSIFSWGVLASLAYQRYKAGVDAFIQNYVDPTPDPTTAYASYPSASVENYQQPPFTQNVETTEGYQPPPVY
| null | null |
protein targeting [GO:0006605]; regulated exocytosis [GO:0045055]; synaptic vesicle membrane organization [GO:0048499]
|
membrane [GO:0016020]; neuromuscular junction [GO:0031594]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
| null |
PF01284;
| null |
Synaptogyrin family
|
PTM: May be tyrosine phosphorylated by Src. {ECO:0000269|PubMed:9446595}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:26071524}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:9446595}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to cytoplasmic vesicles associated with the recycling endosomes. {ECO:0000269|PubMed:10967091}.
| null | null | null | null | null |
FUNCTION: May play a role in regulated exocytosis (PubMed:10383386). In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles (PubMed:12928441, PubMed:15590695). May also play a role in GLUT4 storage and transport to the plasma membrane (PubMed:26071524). {ECO:0000269|PubMed:10383386, ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:15590695, ECO:0000269|PubMed:26071524}.
|
Rattus norvegicus (Rat)
|
O54982
|
KCNU1_MOUSE
|
MSQTLLDSLNQKELTETSCTIEIQAAFILSSLATFFGGLIILFLFRIALKSSRSWKYVKGPRGLLELFSSRRIEANPLRKLYFHGVFRQRIEMLLSAQTVVGQVLVILVFVLSIGSLVIYFINSMDPVRRCSSYEDKIVHGDLSFNAFFSFYFGLRFWAAEDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPKILQILQVIKTSNSVKLSKLLSIVISTWFTAAGFLHLVENSGDPWLNGRNSQTMSYFESIYLVTATMSTVGFGDVVAKTSLGRIFIVFFTLGSLILFANYIPEMVELFSTRKKYTKPYEAVKGKKFIVVCGNITVDSVTAFLRNFLHWKSGEINIEIVFLGETLPCLELETLLKCHTSCTNFVCGTALKFEDLKRVAVENSEACLILANHFCSDLHDEDNSNIMRVLSIKNYYPQTRVIIQILQSQNKVFLSKIPNWDWSAGDNILCFAELKLGFIAQGCLVPGLCTFLTTLFIEQNQKVFPKHPWQKHFLNGLKNKILTQRLSNDFVGMTFPQVSRLCFVKLNLMLIAIQHKPFFHSCCTLILNPSSQVRLNKDTLGFFIADSSKAVKRAFFYCSNCHSDVCNPELIGKCNCKIKSRQQLIAPTIMVMKSSLTDFTTSSHIHASMSTEIHTCFSREQPSLITITTNRPTTNDTVDDTDMLDSSGMFHWCRAMPLDKVVLKRSEKAKHEFQNHIVVCVFGDAQCTLVGLRNFVMPLRASNYTRQELKDIVFIGSLEYFQREWRFLRNFPKIHIMPGSALYMGDLIAVNVEQCSMCVILATPYKALSSQILVDTEAIMATLNIQSLRITSPTPGSSKSEVKPSSAFDSKERKQRYKQIPILTELKNPSNIHFIEQMGGLDGMLKGTSLHLSTSFSTGAVFSDTFLDSLLATSFYNYHVVELLQMLVTGGISSEMEHYLVKEKPYKTTDDYEAIKSGRTRCKLGLLSLDQTVLSGINPRKTFGQLFCGSLDNFGILCVGLYRMIDEEEPSQEHKRFVITRPSNECHLLPSDLVFCAIPFNTTCGKSDSSPSIQAQNNSTNATTPLAQGSNFFDSHHADESHDLYPVDDTGERWSQHHHSRVYPLDTLDASDIVQEK
| null | null |
establishment of localization in cell [GO:0051649]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein stabilization [GO:0050821]; reproductive process [GO:0022414]
|
membrane [GO:0016020]; monoatomic ion channel complex [GO:0034702]; postsynaptic membrane [GO:0045211]
|
potassium channel activity [GO:0005267]
|
PF03493;PF00520;PF21014;
|
1.10.287.70;3.40.50.720;
|
Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa5.1/KCNU1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22084117}; Multi-pass membrane protein {ECO:0000269|PubMed:22084117}.
| null | null | null | null | null |
FUNCTION: Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). Represents the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina. {ECO:0000269|PubMed:11696614, ECO:0000269|PubMed:11723163, ECO:0000269|PubMed:15201331, ECO:0000269|PubMed:16940554, ECO:0000269|PubMed:16940555, ECO:0000269|PubMed:21427226, ECO:0000269|PubMed:23129643, ECO:0000269|PubMed:9452476}.
|
Mus musculus (Mouse)
|
O54983
|
CRYM_MOUSE
|
MKRAPAFLSAEEVQDHLRSSSLLIPPLEAALANFSKGPDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASTVQGDVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQAVLYVDSREAALKESGDVLLSGADIFAELGEVISGAKPAHCEKTTVFKSLGMAVEDLVAAKLVYDSWSSGK
|
1.5.1.25
| null |
mitochondrial transport [GO:0006839]; negative regulation of transcription by RNA polymerase II [GO:0000122]; sensory perception of sound [GO:0007605]; thyroid hormone metabolic process [GO:0042403]; thyroid hormone transport [GO:0070327]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
hormone binding [GO:0042562]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]; thiomorpholine-carboxylate dehydrogenase activity [GO:0047127]; thyroid hormone binding [GO:0070324]; transcription corepressor activity [GO:0003714]
|
PF02423;
|
3.40.50.720;3.30.1780.10;
|
Ornithine cyclodeaminase/mu-crystallin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NAD(+) = 3,4-dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:12504, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873; EC=1.5.1.25; CATALYTIC ACTIVITY: Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NADP(+) = 3,4-dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADPH; Xref=Rhea:RHEA:12500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873; EC=1.5.1.25;
| null | null | null | null |
FUNCTION: Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O54988
|
SLK_MOUSE
|
MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWEIIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSKWSSNFKDFLRKCLEKNVDARWTTSQLLQHPFVTVDSNKPVRELIAEAKAEVTEEVEDGKEEDEEEEAENALPIPANKRASSDLSIASSEEDKLSQNACILESVSERTEQSTSEDKFSNKILNEKPTTDGPEKAVDEHASDVNLETGAELNDQTVGIHENGREKKRPKLENLPDTQDQQTVDVNSVSEENENNRVTLETNTDCLKPEEDRNKENQETLESKLIQSEEINDTHIQTMDLVSQETGEKEADFQAVDNEVGLTKEETQEKLGKDGTAQKVITSDRSSEVGTDEALDDTQKAAELSKAAQSGEGDEALAPTQTLAEKPTEGPEAGGAEEEPPGGERVEDKQPEQQPAVCEAEGQLTSTSETTRATLEQPETDEVEQVSESNSIEELERLVVTGAEARALGSEGEAAATEVDLERKENAQKVPVKAESQAPAASQPSEPHPVLIPSININSETTENKEEMGALPKPETILPPEPEHEKGNDTDSGTGSTVENSSGDLNLSISSFLSKAKDSGSVSLQETRRQKKTLKKTRKFIVDGVEVSVTTSKIVTDSDSKTEELRFLRRQELRELRLLQKEEQRAQQQLNGKLQQQREQIFRRFEQEMLSKKRQYDQEIENLEKQQKQTIERLEQEHTNRLRDEAKRIKGEQEKELSKFQNVLKNRKKEVMNEVEKAPRELRRELTKRRKEELAQSQHAQEQEFVQKQQQELDGSLKKIIQQQKAELANIERECLNNKQQLMRAREAAIWELEERHLQEKHQLLKQQLKDQYFMQRHQLLKRHEKETEQMQRYNQRLIEELKNRQTQERARLPKIQRSEAKTRMAMFKKSLRINSTATPDQDREKIKQFAAQEEKRQKNERMAQHQKHESQMRDLQLQCEANVRELHQLQNEKCHLLVEHETQKLKELDEEHSQELKEWREKLRPRKKTLEEEFARKLQEQEVFFKMTGESECLNPSAQSRISKFYPIPTLHSTGS
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; cellular response to type II interferon [GO:0071346]; cytoplasmic microtubule organization [GO:0031122]; positive regulation of apoptotic process [GO:0043065]; protein autophosphorylation [GO:0046777]; regulation of apoptotic process [GO:0042981]; regulation of cell migration [GO:0030334]; regulation of focal adhesion assembly [GO:0051893]
|
cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
|
ATP binding [GO:0005524]; histone kinase activity [GO:0035173]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF12474;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Proteolytically cleaved by caspase-3. {ECO:0000269|PubMed:10611247}.; PTM: Autophosphorylated. {ECO:0000269|PubMed:9808774}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10611247, ECO:0000269|PubMed:9808774}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Mediates apoptosis and actin stress fiber dissolution. {ECO:0000269|PubMed:10611247}.
|
Mus musculus (Mouse)
|
O54990
|
PROM1_MOUSE
|
MALVFSALLLLGLCGKISSEGQPAFHNTPGAMNYELPTTKYETQDTFNAGIVGPLYKMVHIFLSVVQPNDFPLDLIKKLIQNKKFDISVDSKEPEIIVLALKIALYEIGVLICAILGLLFIILMPLVGCFFCMCRCCNKCGGEMHQRQKQNAPCRRKCLGLSLLVICLLMSLGIIYGFVANQQTRTRIKGTQKLAKSNFRDFQTLLTETPKQIDYVVEQYTNTKNKAFSDLDGIGSVLGGRIKDQLKPKVTPVLEEIKAMATAIKQTKDALQNMSSSLKSLQDAATQLNTNLSSVRNSIENSLSSSDCTSDPASKICDSIRPSLSSLGSSLNSSQLPSVDRELNTVTEVDKTDLESLVKRGYTTIDEIPNTIQNQTVDVIKDVKNTLDSISSNIKDMSQSIPIEDMLLQVSHYLNNSNRYLNQELPKLEEYDSYWWLGGLIVCFLLTLIVTFFFLGLLCGVFGYDKHATPTRRGCVSNTGGIFLMAGVGFGFLFCWILMILVVLTFVVGANVEKLLCEPYENKKLLQVLDTPYLLKEQWQFYLSGMLFNNPDINMTFEQVYRDCKRGRGIYAAFQLENVVNVSDHFNIDQISENINTELENLNVNIDSIELLDNTGRKSLEDFAHSGIDTIDYSTYLKETEKSPTEVNLLTFASTLEAKANQLPEGKPKQAFLLDVQNIRAIHQHLLPPVQQSLNTLRQSVWTLQQTSNKLPEKVKKILASLDSVQHFLTNNVSLIVIGETKKFGKTILGYFEHYLHWVFYAITEKMTSCKPMATAMDSAVNGILCGYVADPLNLFWFGIGKATVLLLPAVIIAIKLAKYYRRMDSEDVYDDVETVPMKNLEIGSNGYHKDHLYGVHNPVMTSPSRY
| null | null |
camera-type eye photoreceptor cell differentiation [GO:0060219]; photoreceptor cell maintenance [GO:0045494]; retina layer formation [GO:0010842]
|
apical plasma membrane [GO:0016324]; brush border [GO:0005903]; cell projection [GO:0042995]; cell surface [GO:0009986]; cilium [GO:0005929]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular space [GO:0005615]; microvillus [GO:0005902]; microvillus membrane [GO:0031528]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; prominosome [GO:0071914]; stereocilium [GO:0032420]
|
cholesterol binding [GO:0015485]
|
PF05478;
| null |
Prominin family
|
PTM: Acetylation at Lys-226, Lys-258 and Lys-265 by NAT8 and NAT8B may control PROM1 protein expression and its function in cell apoptosis.
|
SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. Cell projection, microvillus membrane; Multi-pass membrane protein. Cell projection, cilium, photoreceptor outer segment. Endoplasmic reticulum {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Found in extracellular membrane particles in various body fluids such as ventricular fluid of the developing brain and urine.
| null | null | null | null | null |
FUNCTION: May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis (PubMed:19228982). Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner. {ECO:0000269|PubMed:19228982}.
|
Mus musculus (Mouse)
|
O54991
|
CNTP1_MOUSE
|
MMSLRLFSILLATVVSGAWGWGYYGCNEELVGPLYARSLGASSYYGLFTTARFARLHGISGWSPRIGDPNPWLQIDLMKKHRIRAVATQGAFNSWDWVTRYMLLYGDRVDSWTPFYQKGHNATFFGNVNDSAVVRHDLHYHFTARYIRIVPLAWNPRGKIGLRLGIYGCPYTSSILYFDGDDAISYRFQRGASQSLWDVFAFSFKTEEKDGLLLHTEGSQGDYVTLELQGAHLLLHMSLGSSPIQPRPGHTTVSLGGVLNDLSWHYVRVDRYGRDANFTLDGYAHHFVLNGDFERLNLENEIFIGGLVGAARKNLAYRHNFRGCIENVIYNRINIAEMAVMRHSRITFEGNVAFRCLDPVPHPINFGGPHNFVQVPGFPRRGRLAVSFRFRTWDLTGLLLFSHLGDGLGHVELMLSEGQVNVSIAQTGRKKLQFAAGYRLNDGFWHEVNFVAQENHAVISIDDVEGAEVRVSYPLLIRTGTSYFFGGCPKPASRWGCHSNQTAFHGCMELLKVDGQLVNLTLVEFRKLGYFAEVLFDTCGITDRCSPNMCEHDGRCYQSWDDFICYCELTGYKGVTCHEPLYKESCEAYRLSGKYSGNYTIDPDGSGPLKPFVVYCDIRENRAWTVVRHDRLWTTRVTGSSMDRPFLGAIQYWNASWEEVSALANASQHCEQWIEFSCYNSRLLNTAGGYPYSFWIGRNEEQHFYWGGSQPGIQRCACGLDQSCVDPALHCNCDADQPQWRTDKGLLTFVDHLPVTQVVVGDTNRSNSEAQFFLRPLRCYGDRNSWNTISFHTGAALRFPPIRANHSLDVSFYFRTSAPSGVFLENMGGPFCRWRRPYVRVELNTSRDVVFAFDIGNGDENLTVHSDDFEFNDDEWHLVRAEINVKQARLRVDHRPWVLRPMPLQTYIWLVYDQPLYVGSAELKRRPFVGCLRAMRLNGVTLNLEGRANASEGTFPNCTGHCTHPRFPCFHGGRCVERYSYYTCDCDLTAFDGPYCNHDIGGFFETGTWMRYNLQSALRSAAREFSHMLSRPVPGYEPGYVPGYDTPGYVPGYHGPGYRLPEYPRPGRPVPGYRGPVYNVTGEEVSFSFSTNSAPAVLLYVSSFVRDYMAVLIKEDGTLQLRYQLGTSPYVYQLTTRPVTDGQPHSVNITRVYRNLFIQVDYFPLTEQKFSLLVDSQLDSPKALYLGRVMETGVIDPEIQRYNTPGFSGCLSGVRFNNVAPLKTHFRTPRPMTAELAEAMRVQGELSESNCGAMPRLVSEVPPELDPWYLPPDFPYYHDDGWIAILLGFLVAFLLLGLVGMLVLFYLQNHRYKGSYHTNEPKATHDSHPGGKAPLPPSGPAQAPAPTPAPTQLPTPAPAPAPAPASGPGPRDQNLPQILEESRSE
| null | null |
axonogenesis [GO:0007409]; cell adhesion [GO:0007155]; central nervous system myelination [GO:0022010]; cytoskeleton organization [GO:0007010]; mitochondrion organization [GO:0007005]; myelination [GO:0042552]; myelination in peripheral nervous system [GO:0022011]; neuromuscular junction development, skeletal muscle fiber [GO:0098529]; neuromuscular process [GO:0050905]; neuromuscular process controlling balance [GO:0050885]; neuromuscular process controlling posture [GO:0050884]; neuron projection development [GO:0031175]; neuron projection morphogenesis [GO:0048812]; neuronal action potential propagation [GO:0019227]; paranodal junction assembly [GO:0030913]; paranodal junction maintenance [GO:1990227]; postsynaptic density organization [GO:0097106]; protein localization to juxtaparanode region of axon [GO:0071205]; protein localization to paranode region of axon [GO:0002175]; regulation of synapse maturation [GO:0090128]
|
axon [GO:0030424]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; myelin sheath [GO:0043209]; paranodal junction [GO:0033010]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; presynaptic active zone [GO:0048786]; septate junction [GO:0005918]
|
SH3 domain binding [GO:0017124]
|
PF00754;PF02210;
|
2.60.120.1000;2.60.120.200;2.60.120.260;2.10.25.10;
|
Neurexin family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, paranodal septate junction {ECO:0000269|PubMed:25378149}.
| null | null | null | null | null |
FUNCTION: Required, with CNTNAP2, for radial and longitudinal organization of myelinated axons (PubMed:25378149). Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the paranodal region of the axo-glial junction. In association with contactin involved in the signaling between axons and myelinating glial cells (PubMed:11395000, PubMed:25378149). {ECO:0000269|PubMed:11395000, ECO:0000269|PubMed:25378149}.
|
Mus musculus (Mouse)
|
O54992
|
MAPK5_MOUSE
|
MSEDSDMEKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALQHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRKKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDGIYIHDHENGTEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDALQSFSWNGRGFTDKVDRLKLAEVVKQVIEEQTLPHEPQ
|
2.7.11.1
| null |
negative regulation of TOR signaling [GO:0032007]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; protein autophosphorylation [GO:0046777]; Ras protein signal transduction [GO:0007265]; regulation of translation [GO:0006417]; stress-induced premature senescence [GO:0090400]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; septin cytoskeleton [GO:0032156]
|
ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019]; p53 binding [GO:0002039]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
4.10.1170.10;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
|
PTM: Phosphorylated on Thr-182 ERK3/MAPK6 or ERK4/MAPK4; which is the regulatory phosphorylation site and is located on the T-loop/loop 12, leading to activation. Phosphorylation at Thr-182 by p38-alpha/MAPK14, p38-beta/MAPK11 is subject to debate. Phosphorylated at Ser-115 by PKA/PRKACA, leading to localization to the cytoplasm. Autophosphorylated. {ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:15577943, ECO:0000269|PubMed:20734105, ECO:0000269|PubMed:9480836}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20640477}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20640477};
| null | null | null | null |
FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement. {ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:15577943, ECO:0000269|PubMed:16973613, ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:21336308, ECO:0000269|PubMed:21575178}.
|
Mus musculus (Mouse)
|
O54998
|
FKBP7_MOUSE
|
MNLLFRLAVFLSLWCCSDAQGQTKEESTEEVKIEVLHRPENCSKTSRKGDLLNAHYDGYLAKDGSKFYCSRTQDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGYAEGKIPPNATLMFEIELYAVTKGPRSIETFKQIDTDNDRQLSKAEIELYLQKDFEKDANPRDKSYQKAVLEDIFKKNDHNGDGFISPKEYNVHQHDEL
|
5.2.1.8
| null | null |
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]
|
calcium ion binding [GO:0005509]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]
|
PF13499;PF00254;
|
3.10.50.40;1.10.238.10;
| null |
PTM: Glycosylated. {ECO:0000269|PubMed:9806833}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:9806833}.
|
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
| null | null | null | null |
FUNCTION: PPIases accelerate the folding of proteins during protein synthesis.
|
Mus musculus (Mouse)
|
O55000
|
PP1RA_RAT
|
MGSGPIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKEEGKSRTTLPERPLTEVKAETRAEEAPEKKKEKPKSLRTTAPSHAKFRSTGLELDTPSLVPVKKNSSTVVVSDKYNLKPIPLKRQSATAAPGDAAPPAEKKYKPLNTTPNTTKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAAPAEPMDTDRPGTPVPAVEVPELMDAASSEPGALDAKPVESPGDPNQLTRKGRKRKTVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVIPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECAMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKSPQGPGGGGINVQEILTSIMGSPNNHPSEELLKQPDYSDKLKQMLVPHGLLGPGPVANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPSRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPFRGARGGRSGGGPPNGRGGPGGGGMVGGGGHRPHEGPGGSMGSGHRSHEGPGGSMGSGHRSHEGPGHGGPHGHRPHDVPSHRGHDHRGPPPHEHRGHDGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP
| null | null |
negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of mitotic DNA damage checkpoint [GO:1904290]; positive regulation of telomere maintenance [GO:0032206]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; nuclear body [GO:0016604]; PTW/PP1 phosphatase complex [GO:0072357]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase inhibitor activity [GO:0004864]; RNA binding [GO:0003723]
|
PF08711;PF00642;
|
1.20.930.10;
| null |
PTM: Phosphorylated on Thr-398 by PKA within the region necessary for interaction with PPP1CA. {ECO:0000269|PubMed:12574161}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}. Note=Found in discrete nucleoplasmic bodies and within nucleoli. Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers. {ECO:0000269|PubMed:12574161, ECO:0000269|PubMed:9461602}.
|
Rattus norvegicus (Rat)
|
O55003
|
BNIP3_MOUSE
|
MSQSGEENLQGSWVELHFSNGNGSSVPASVSIYNGDMEKILLDAQHESGRSSSKSSHCDSPPRSQTPQDTNRAEIDSHSFGEKNSTLSEEDYIERRREVESILKKNSDWIWDWSSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSADFLKVFLPSLLLSHLLAIGLGIYIGRRLTTSTSTF
| null | null |
apoptotic process [GO:0006915]; autophagic cell death [GO:0048102]; brown fat cell differentiation [GO:0050873]; cardiac muscle cell apoptotic process [GO:0010659]; cellular response to cobalt ion [GO:0071279]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to mechanical stimulus [GO:0071260]; cerebral cortex development [GO:0021987]; defense response to virus [GO:0051607]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to hypoxia [GO:1990144]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial outer membrane permeabilization [GO:0097345]; mitochondrial protein catabolic process [GO:0035694]; negative regulation of apoptotic process [GO:0043066]; negative regulation of membrane potential [GO:0045837]; negative regulation of mitochondrial fusion [GO:0010637]; negative regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902109]; negative regulation of mitochondrial membrane potential [GO:0010917]; negative regulation of programmed cell death [GO:0043069]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; neuron apoptotic process [GO:0051402]; oligodendrocyte differentiation [GO:0048709]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy of mitochondrion [GO:1903599]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of macroautophagy [GO:0016239]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of programmed cell death [GO:0043068]; positive regulation of protein-containing complex disassembly [GO:0043243]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; reactive oxygen species metabolic process [GO:0072593]; regulation of aerobic respiration [GO:1903715]; regulation of mitochondrial membrane permeability [GO:0046902]; regulation of mitochondrion organization [GO:0010821]; response to axon injury [GO:0048678]; response to bacterium [GO:0009617]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to oxygen-glucose deprivation [GO:0090649]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]
|
GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF06553;
|
6.10.250.1020;
|
NIP3 family
| null |
SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the mitochondrion outer membrane (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2 (By similarity). Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane may play a critical role in the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O55005
|
ROBO1_RAT
|
MKWKHLPLLVMISLLTLSKKHLLLAQLIPDPEDLERGNDNGTPAPTSDNDDNSLGYTGSRLRQEDFPPRIVEHPSDLIVSKGEPATLNCKAEGRPTPTIEWYKGGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRKSRPDEGVYICVARNYLGEAVSHNASLEVAILRDDFRQNPSDVMVAVGEPAVMECQPPRGHPEPTISWKKDGSPLDDKDERITIRGGKLMITYTRKSDAGKYVCVGTNMVGERESKVADVTVLERPSFVKRPSNLAVTVDDSAEFKCEARGDPVPTFGWRKDDGELPKSRYEIRDDHTLKIRKVTAGDMGSYTCVAENMVGKAEASATLTVQEPPHFVVKPRDQVVALGRTVTFQCEATGNPQPAIFWRREGSQNLLFSYQPPQSSSRFSVSQTGDLTVTNVQRSDVGYYICQTLNVAGSIITKAYLEVTDVIADRPPPVIRQGPVNQTVAVDGTLTLSCVATGSPVPTILWRKDGVLVSTQDSRIKQLESGVLQIRYAKLGDTGRYTCTASTPSGEATWSAYIEVQEFGVPVQPPRPTDPNLIPSAPSKPEVTDVSKNTVTLLWQPNLNSGATPTSYIIEAFSHASGSSWQTVAENVKTETFAIKGLKPNAIYLFLVRAANAYGISDPSQISDPVKTQDVPPTTQGVDHKQVQRELGNVVLHLHNPTILSSSSVEVHWTVDQQSQYIQGYKILYRPSGASHGESEWLVFEVRTPTKNSVVIPDLRKGVNYEIKARPFFNEFQGADSEIKFAKTLEERPSAPPRSVTVSKNDGNGTAILVTWQPPPEDTQNGMVQEYKVWCLGNETRYHINKTVDGSTFSVVIPFLVPGIRYSVEVAASTGAGPGVKSEPQFIQLDSHGNPVSPEDQVSLAQQISDVVKQPAFIAGIGAACWIILMVFSIWLYRHRKKRNGLSSTYAGIRKVPSFTFTPTVTYQRGGEAVSSGGRPGLLNISEPATQPWLADTWPNTGNSHNDCSINCCTASNGNSDSNLTTYSRPADCIANYNNQLDNKQTNLMLPESTVYGDVDLSNKINEMKTFNSPNLKDGRFVNPSGQPTPYATTQLIQANLINNMNNGGGDSSEKHWKPPGQQKQEVAPIQYNIMEQNKLNKDYRANDTILPTIPYNHSYDQNTGGSYNSSDRGSSTSGSQGHKKGARTPKAPKQGGMNWADLLPPPPAHPPPHSNSEEYSMSVDESYDQEMPCPVPPARMYLQQDELEEEEAERGPTPPVRGAASSPAAVSYSHQSTATLTPSPQEELQPMLQDCPEDLGHMPHPPDRRRQPVSPPPPPRPISPPHTYGYISGPLVSDMDTDAPEEEEDEADMEVAKMQTRRLLLRGLEQTPASSVGDLESSVTGSMINGWGSASEEDNISSGRSSVSSSDGSFFTDADFAQAVAAAAEYAGLKVARRQMQDAAGRRHFHASQCPRPTSPVSTDSNMSAAVIQKARPTKKQKHQPGHLRREAYTDDLPPPPVPPPAIKSPSVQSKAQLEARPIMGPKLASIEARADRSSDRKGGSYKGREALDGRQVTDLRTSPGDPREAQEQPNEGKARGTKTAKRDLPPAKTHLIPEDILPYCRPTFPTSNNPRDPSSSSSMSSRGSGSRQREQANVGRRNMAEMQVLGGFERGDENNEELEETES
| null | null |
aorta development [GO:0035904]; aortic valve morphogenesis [GO:0003180]; axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to hypoxia [GO:0071456]; chemorepulsion involved in postnatal olfactory bulb interneuron migration [GO:0021836]; coronary vasculature development [GO:0060976]; endocardial cushion formation [GO:0003272]; heart development [GO:0007507]; heart induction [GO:0003129]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; kidney development [GO:0001822]; mammary duct terminal end bud growth [GO:0060763]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chemokine-mediated signaling pathway [GO:0070100]; negative regulation of gene expression [GO:0010629]; negative regulation of mammary gland epithelial cell proliferation [GO:0033600]; negative regulation of negative chemotaxis [GO:0050925]; negative regulation of synapse assembly [GO:0051964]; neuron projection extension [GO:1990138]; olfactory bulb interneuron development [GO:0021891]; oligodendrocyte development [GO:0014003]; outflow tract septum morphogenesis [GO:0003148]; positive regulation of axonogenesis [GO:0050772]; positive regulation of gene expression [GO:0010628]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; positive regulation of vascular endothelial growth factor signaling pathway [GO:1900748]; pulmonary valve morphogenesis [GO:0003184]; regulation of dendrite morphogenesis [GO:0048814]; Roundabout signaling pathway [GO:0035385]; spinal cord development [GO:0021510]; synapse organization [GO:0050808]; ventricular septum development [GO:0003281]; ventricular septum morphogenesis [GO:0060412]
|
axolemma [GO:0030673]; axon [GO:0030424]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
axon guidance receptor activity [GO:0008046]; identical protein binding [GO:0042802]; LRR domain binding [GO:0030275]
|
PF00041;PF07679;PF13927;
|
2.60.40.10;
|
Immunoglobulin superfamily, ROBO family
|
PTM: Ubiquitinated. May be deubiquitinated by USP33. {ECO:0000250|UniProtKB:O89026}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28859078}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9Y6N7}. Cell projection, axon {ECO:0000250|UniProtKB:O89026}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:28859078}; Single-pass membrane protein {ECO:0000305|PubMed:28859078}. Note=Detected at growth cones in thalamus neurons (By similarity). PRRG4 prevents cell surface location and both colocalize in the Endoplasmic reticulum/Golgi adjacent to the cell nucleus (PubMed:28859078). {ECO:0000250|UniProtKB:O89026, ECO:0000269|PubMed:28859078}.
| null | null | null | null | null |
FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (By similarity). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (By similarity). {ECO:0000250|UniProtKB:O89026, ECO:0000250|UniProtKB:Q9Y6N7}.
|
Rattus norvegicus (Rat)
|
O55012
|
PICAL_RAT
|
MSGQSLTDRITAAQHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDFTKVKRGADGVMRTMNTEKLLKTVPIIQNQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLKVAEQVGIDRGDIPDLSQAPSSLLDALEQHLASLEGKKIKDSTAASRATTLSNAVSSLASTGLSLTKVDEREKQAALEEEQARLKALKEQRLKELAKKPHTSLTTAASPVSTSAGGIMTAPAIDIFSTPSSSNSTSKLPNDLLDLQQPTFHPSVHAMSAAPQVASTWGDAVDDAIPSLNPFLTKSSGDVHLPISSDVSTFTTRTPTHEMFVGFSPSPVTQPHPSAGLNVDFESVFGNKSTNVAVDSGGGLLKPTVASQNQSLPVAKLPPNKLVSDDLDSSLANLVGNLGIGNGTTKNDVSCSQPGEKKLTGGSNWQPKVAPTTAWSAATMAPPVMAYPATTPTGMIGYGIPPQMGSVPVMTQPTLIYSQPVMRPPNPFGPVPGAQIQFM
| null | null |
amyloid-beta clearance by transcytosis [GO:0150093]; axonogenesis [GO:0007409]; clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; dendrite morphogenesis [GO:0048813]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; hemopoiesis [GO:0030097]; intracellular iron ion homeostasis [GO:0006879]; learning or memory [GO:0007611]; membrane bending [GO:0097753]; multicellular organismal-level iron ion homeostasis [GO:0060586]; negative regulation of gene expression [GO:0010629]; negative regulation of protein localization to cell surface [GO:2000009]; negative regulation of protein localization to plasma membrane [GO:1903077]; negative regulation of receptor-mediated endocytosis [GO:0048261]; positive regulation of amyloid precursor protein catabolic process [GO:1902993]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of axonogenesis [GO:0050772]; positive regulation of dendrite extension [GO:1903861]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of synaptic vesicle clustering [GO:2000809]; positive regulation of synaptic vesicle endocytosis [GO:1900244]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; regulation of amyloid precursor protein catabolic process [GO:1902991]; regulation of endocytosis [GO:0030100]; regulation of protein localization [GO:0032880]; regulation of protein transport [GO:0051223]; regulation of synaptic vesicle endocytosis [GO:1900242]; regulation of synaptic vesicle transport [GO:1902803]; regulation of terminal button organization [GO:2000331]; regulation of vesicle size [GO:0097494]; synaptic vesicle budding from presynaptic endocytic zone membrane [GO:0016185]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle maturation [GO:0016188]; vesicle budding from membrane [GO:0006900]; vesicle cargo loading [GO:0035459]; vesicle-mediated transport [GO:0016192]
|
cell surface [GO:0009986]; clathrin coat of coated pit [GO:0030132]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome to plasma membrane transport vesicle [GO:0070381]; extrinsic component of presynaptic endocytic zone membrane [GO:0098894]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; neurofibrillary tangle [GO:0097418]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic vesicle [GO:0008021]; vesicle [GO:0031982]
|
1-phosphatidylinositol binding [GO:0005545]; clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; identical protein binding [GO:0042802]; low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; SH3 domain binding [GO:0017124]; small GTPase binding [GO:0031267]; SNARE binding [GO:0000149]; tau protein binding [GO:0048156]
|
PF07651;
|
1.25.40.90;1.20.58.150;
|
PICALM/SNAP91 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13492}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q13492}. Golgi apparatus {ECO:0000250|UniProtKB:Q13492}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q13492}. Nucleus {ECO:0000250|UniProtKB:Q13492}. Note=Colocalized with clathrin in the Golgi area. Interaction with PIMREG may target PICALM to the nucleus in some cells. {ECO:0000250|UniProtKB:Q13492}.
| null | null | null | null | null |
FUNCTION: Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane leading to clathrin-coated vesicles (CCVs) assembly. Furthermore, regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature. In addition to binding to clathrin, mediates the endocytosis of small R-SNARES (Soluble NSF Attachment Protein REceptors) between plasma membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8. In turn, PICALM-dependent SNARE endocytosis is required for the formation and maturation of autophagic precursors. Modulates thereby autophagy and the turnover of autophagy substrates such as MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-CTF). {ECO:0000250|UniProtKB:Q13492, ECO:0000269|PubMed:11190274}.
|
Rattus norvegicus (Rat)
|
O55013
|
TPPC3_MOUSE
|
MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDRMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSALIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE
| null | null |
COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; vesicle coating [GO:0006901]; vesicle tethering [GO:0099022]
|
cis-Golgi network membrane [GO:0033106]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]; TRAPP complex [GO:0030008]; TRAPPII protein complex [GO:1990071]; TRAPPIII protein complex [GO:1990072]
| null |
PF04051;
|
3.30.1380.20;
|
TRAPP small subunits family, BET3 subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
|
Mus musculus (Mouse)
|
O55017
|
CAC1B_MOUSE
|
MVRFGDELGGRYGGTGGGERARGGGAGGAGGPGQGGLPPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDTEPVGDFPCGKDPPARQCDGDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDKNAEEKSPLDVLKRAATKKSRNDLIHAEEGEDRFVDLCAVGSPFARASLKSGKTESSSYFRRKEKMFRFFIRRMVKAQSFYWVVLCVVALNTLCVAMVHYNQPQRLTTALYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSIFEVVWAAIKPGTSFGISVLRALRLLRIFKVTKYWNSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFQDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSKGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRYASTRHVRPDMKTHMDRPLVVEPGRDGLRGPVGSKSKPEGTEATESADLPRRHHRHRDRDKTSATAPAGGEQDRTESTETGAREERARPRRSHSKETPGADTQVRCERSRRHHRRGSPEEATEREPRRHRAHRHAQDSSKEGTAPVLVPKGERRARHRGPRTGPREAENNEEPTRRHRARHKVPPTLQPPEREAAEKESNAVEGDKETRNHQPKEPHCDLEAIAVTGVGPLHMLPSTCLQKVDEQPEDADNQRNVTRMGSQPSDPSTTVHVPVTLTGPPGETPVVPSGNMNLEGQAEGKKEAEADDVLRRGPRPIVPYSSMFCLSPTNLLRRFCHYIVTMRYFEMVILVVIALSSIALAAEDPVRTDSFRNNALKYMDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSSFMGGSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGFRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISAKPLTRYMPQNKQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSMECILKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIANNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDDTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLGNRACDPHANASECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYNDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISNEDMTVHFTSTLMALIRTALEIKLAPAGTKQHQCDAELRKEISSVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTTRDQTHQAPGGLSQMGPVSLFHPLKATLEQTQPAVLRGARVFLRQKSATSLSNGGAIQTQESGIKESLSWGTQRTQDALYEARAPLERGHSAEIPVGQSGTLAVDVQMQNMTLRGPDGEPQPGLESQGRAASMPRLAAETQPAPNASPMKRSISTLAPRPHGTQLCSTVLDRPPPSQASHHHHHRCHRRRDKKQRSLEKGPSLSVDPEGAPSTAAGPGLPHGEGSTACRRDRKQERGRSQERRQPSSSSSEKQRFYSCDRFGSREPPQLMPSLSSHPTSPTAALEPAPHPQGSGSVNGSPLMSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPVHFAEGQSGLPAFSPGRLSRGLSEHNALLQKEPLSQPLAPGSRIGSDPYLGQRLDSEASAHTLPEDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSTGVRARHSYHHPDQDHWC
| null | null |
calcium ion import [GO:0070509]; calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; chemical synaptic transmission [GO:0007268]; establishment of localization in cell [GO:0051649]; locomotory behavior [GO:0007626]; neurotransmitter secretion [GO:0007269]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of blood pressure [GO:0008217]; regulation of calcium ion transport [GO:0051924]; regulation of calcium-dependent activation of synaptic vesicle fusion [GO:0150037]; regulation of heart contraction [GO:0008016]; response to organic cyclic compound [GO:0014070]; response to pain [GO:0048265]; response to testosterone [GO:0033574]
|
axon terminus [GO:0043679]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; presynaptic active zone [GO:0048786]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685]; voltage-gated calcium channel complex [GO:0005891]
|
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; high voltage-gated calcium channel activity [GO:0008331]; protein phosphatase 2A binding [GO:0051721]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels [GO:0099626]
|
PF08763;PF16905;PF00520;
|
1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1B subfamily
|
PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q00975}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q00975}.
| null | null | null | null | null |
FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. This alpha-1B subunit gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group. They are involved in pain signaling. Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons. Mediates Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity). {ECO:0000250|UniProtKB:Q02294}.
|
Mus musculus (Mouse)
|
O55022
|
PGRC1_MOUSE
|
MAAEDVVATGADPSELEGGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPGASGDNDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLSDWDSQFTFKYHHVGKLLKEGEEPTVYSDDEEPKDETARKNE
| null | null |
associative learning [GO:0008306]; heme biosynthetic process [GO:0006783]; memory [GO:0007613]; modification of synaptic structure [GO:0099563]; negative regulation of synapse organization [GO:1905809]; positive regulation of lipoprotein transport [GO:0140077]; positive regulation of protein localization to plasma membrane [GO:1903078]
|
cell body [GO:0044297]; endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; synapse [GO:0045202]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; steroid binding [GO:0005496]
|
PF00173;
|
3.10.120.10;
|
Cytochrome b5 family, MAPR subfamily
|
PTM: O-glycosylated; contains chondroitin sulfate attached to Ser-54. Ser-54 is in the cytoplasmic domain but the glycosylated form was detected in urine, suggesting that the membrane-bound form is cleaved, allowing for production of a secreted form which is glycosylated. {ECO:0000250|UniProtKB:O00264}.
|
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00264}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:27599036}; Single-pass membrane protein {ECO:0000305}; Extracellular side {ECO:0000269|PubMed:27599036}. Secreted {ECO:0000250|UniProtKB:O00264}.
| null | null | null | null | null |
FUNCTION: Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (PubMed:28005395). Intracellular heme chaperone. Regulates heme synthesis via interactions with FECH and acts as a heme donor for at least some hemoproteins (PubMed:27599036). Forms a ternary complex with TMEM97 receptor and low density lipid receptor/LDLR, which increases LDLR-mediated LDL lipoprotein internalization (By similarity). {ECO:0000250|UniProtKB:O00264, ECO:0000269|PubMed:27599036, ECO:0000269|PubMed:28005395}.
|
Mus musculus (Mouse)
|
O55023
|
IMPA1_MOUSE
|
MADPWQECMDYAVILARQAGEMIREALKNEMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTESPTWFIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRKPETLRIVLSNMEKLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVTEAGGVLMDVTGGPFDLMSRRIIAANSITLAKRIAKEIEIIPLQRDDES
|
3.1.3.25; 3.1.3.94
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000303|PubMed:23027737};
|
inositol biosynthetic process [GO:0006021]; inositol metabolic process [GO:0006020]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; signal transduction [GO:0007165]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]
|
inositol monophosphate 1-phosphatase activity [GO:0008934]; inositol monophosphate 3-phosphatase activity [GO:0052832]; inositol monophosphate 4-phosphatase activity [GO:0052833]; inositol monophosphate phosphatase activity [GO:0052834]; lithium ion binding [GO:0031403]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803]
|
PF00459;
|
3.40.190.80;3.30.540.10;
|
Inositol monophosphatase superfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
|
CATALYTIC ACTIVITY: Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate; Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268, ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25; Evidence={ECO:0000250|UniProtKB:P29218}; CATALYTIC ACTIVITY: Reaction=alpha-D-galactose 1-phosphate + H2O = D-galactose + phosphate; Xref=Rhea:RHEA:29315, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58336; EC=3.1.3.94; Evidence={ECO:0000250|UniProtKB:P29218};
| null |
PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
| null | null |
FUNCTION: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. {ECO:0000250|UniProtKB:P29218}.
|
Mus musculus (Mouse)
|
O55026
|
ENTP2_MOUSE
|
MAGKLVSLVPPLLLAAVGLAGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVRGGGISSYANDPSRAGQSLVECLEQALRDVPKDRYASTPLYLGATAGMRLLNLTSPEATAKVLEAVTQTLTRYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPDNEVHLRLYGQHYRVYTHSFLCYGRDQVLQRLLASALQIHRFHPCWPKGYSTQVLLREVYQSPCTMGQRPQTFNSSATVSLSGTSNAALCRDLVSGLFNISSCPFSQCSFNGVFQPPVAGNFIAFSAFYYTVDFLKTVMGLPVGTLKQLEDATETTCNQTWAELQARVPGQQTRLPDYCAVAMFIHQLLSRGYRFDERSFRGVVFEKKAADTAVGWALGYMLNLTNLIPADLPGLRKGTHFSSWVALLLLFTVLILAALVLLLRQVRSAKSPGAL
|
3.6.1.-
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
cellular response to interleukin-6 [GO:0071354]; G protein-coupled receptor signaling pathway [GO:0007186]; nucleoside diphosphate catabolic process [GO:0009134]; platelet activation [GO:0030168]; purine ribonucleoside diphosphate catabolic process [GO:0009181]
|
basement membrane [GO:0005604]; cell body [GO:0044297]; cell projection membrane [GO:0031253]; cell surface [GO:0009986]; plasma membrane [GO:0005886]
|
ADP phosphatase activity [GO:0043262]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; GDP phosphatase activity [GO:0004382]; identical protein binding [GO:0042802]; nucleoside diphosphate phosphatase activity [GO:0017110]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134]
|
PF01150;
|
3.30.420.40;3.30.420.150;
|
GDA1/CD39 NTPase family
| null |
SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O55028
|
BCKD_MOUSE
|
MILTSVLGSGPRSWSSLWPLLGSSLSLRARSTSATDTHHVELARERSKTVTSFYNQSAIDVAAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIQDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRINPLFGHLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
|
2.7.11.1; 2.7.11.4
| null |
branched-chain amino acid catabolic process [GO:0009083]; isoleucine catabolic process [GO:0006550]; leucine catabolic process [GO:0006552]; lipid biosynthetic process [GO:0008610]; phosphorylation [GO:0016310]; regulation of glucose metabolic process [GO:0010906]; spermatogenesis [GO:0007283]; valine catabolic process [GO:0006574]
|
mitochondrial oxoglutarate dehydrogenase complex [GO:0009353]; mitochondrion [GO:0005739]
|
[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity [GO:0047323]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine phosphatase activity [GO:0004722]; pyruvate dehydrogenase (acetyl-transferring) kinase activity [GO:0004740]
|
PF10436;PF02518;
|
1.20.140.20;3.30.565.10;
|
PDK/BCKDK protein kinase family
|
PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O14874}.
|
SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion {ECO:0000250|UniProtKB:O14874}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase]; Xref=Rhea:RHEA:17301, Rhea:RHEA-COMP:13695, Rhea:RHEA-COMP:13696, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.4; Evidence={ECO:0000250|UniProtKB:O14874}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17302; Evidence={ECO:0000250|UniProtKB:O14874}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O14874}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:O14874};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with PPM1K, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (By similarity). Phosphorylates and inactivates mitochondrial BCKDH complex a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Associates with the E2 component of BCKDH complex and phosphorylates BCKDHA on Ser-334, leading to conformational changes that interrupt substrate channeling between E1 and E2 and inactivates the BCKDH complex (By similarity). Phosphorylates ACLY on Ser-455 in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and glucogenesis, respectively (By similarity). Recognizes phosphosites having SxxE/D canonical motif (By similarity). {ECO:0000250|UniProtKB:O14874}.
|
Mus musculus (Mouse)
|
O55029
|
COPB2_MOUSE
|
MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKGFQPSRPTAQQEPDGKPASSPVIMASQTTHKEEKSLLELEVDLDNLELEDIDTTDINLDEDILDD
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
COPI vesicle coat [GO:0030126]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
protein kinase C binding [GO:0005080]; structural molecule activity [GO:0005198]
|
PF04053;PF00400;
|
1.25.40.470;2.130.10.10;
|
WD repeat COPB2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250|UniProtKB:P35606}.; FUNCTION: This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner.
|
Mus musculus (Mouse)
|
O55033
|
NCK2_MOUSE
|
MTEEVIVIAKWDYTAQQDQELDIRKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKNSLKKGSLVKNLKDTLGLGKTRRKPSARDASPTPSTDAEYPANGSGADRIYDLNIPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSFNGQIGWFPSNYVLEEADEAAAEAPSFLSLRRGTALSNGQGARVLHVVQTLYPFSSVTEEELSFEKGETMEVIEKPENDPEWWKCKNARGQVGLVPKNYVVVLSDGPALHPAHTPQISYTGPSASGRFAGREWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDFSVSLKASGRNKHFKVQLVDSVYCIGQRRFHSMDELVEHYKKAPIFTSEHGEKLYLVRALQ
| null | null |
actin filament organization [GO:0007015]; cell migration [GO:0016477]; dendritic spine development [GO:0060996]; ephrin receptor signaling pathway [GO:0048013]; immunological synapse formation [GO:0001771]; lamellipodium assembly [GO:0030032]; negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation [GO:1903912]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of peptidyl-serine dephosphorylation [GO:1902310]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translation in response to endoplasmic reticulum stress [GO:0036493]; response to endoplasmic reticulum stress [GO:0034976]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; postsynaptic density [GO:0014069]; synapse [GO:0045202]; vesicle membrane [GO:0012506]
|
phosphotyrosine residue binding [GO:0001784]; protein-containing complex binding [GO:0044877]; receptor tyrosine kinase binding [GO:0030971]; scaffold protein binding [GO:0097110]; signaling adaptor activity [GO:0035591]
|
PF00017;PF00018;PF14604;
|
3.30.505.10;2.30.30.40;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O55034
|
SPAG4_RAT
|
MRRNPRPGSAASSHNHTPNFYSENSNSSHSATSGDSNGRRSAGPELGEPDGRMARGSSCGEPALSSGVPGGDTWAGSSRPKLAPRSHNGQTACGAATVRGGASEPSGSPAVLEEQLNLLPILDLRQEMPPPPVSKSFLSLFFQVLSVFLSLVADGLVCVYREICSIRFLFTAVSLLSIFLAALWWGLLYLIPPLENEPKEMLTLSQYHHRVHSQGQQLQQLQAELSKLHKEVTSVRAAHSERVAKLVFQRLNEDFVRKPDYALSSVGASIDLEKTSSDYEDRNTAYFWNRLSFWNYARPPSVILEPDVFPGNCWAFEGEQGQVVIRLPGHVQLSDITLQHPPPTVAHTGGASSAPRDFAVFGLQADDDETEVFLGKFIFEVQKSEIQTFHLQNDPPSAFPKVKIQILSNWGHPRFTCLYRVRAHGVRISESAEDNAMGVTGGPH
| null | null |
cell differentiation [GO:0030154]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; meiotic nuclear membrane microtubule tethering complex [GO:0034993]; microtubule [GO:0005874]; motile cilium [GO:0031514]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]
|
identical protein binding [GO:0042802]; protein-membrane adaptor activity [GO:0043495]
|
PF07738;
|
2.60.120.260;
| null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10373309}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:10373309}. Nucleus envelope {ECO:0000250|UniProtKB:Q9JJF2}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9JJF2}. Note=In spermatids, it is localized in the transient manchette and in the axoneme of elongating spermatids and epididymal sperm. {ECO:0000269|PubMed:10373309}.
| null | null | null | null | null |
FUNCTION: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity (By similarity). May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail (PubMed:10373309). {ECO:0000250|UniProtKB:Q9JJF2, ECO:0000305|PubMed:10373309}.
|
Rattus norvegicus (Rat)
|
O55035
|
PPIG_RAT
|
MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELVPKSKVKKEEKKRHKSSSSSSSSDSDSSSDSQSSSDSSDSESASEEKSRKRKKKHRKNSRKHKKEKKKRKKSKKSPSSESEADNVDAQPQSTVRPEEIPPIPENRFLMRKSPPKADDKERKNRERERERECNPPNSQPASYQRRFLVTRFGRKIKGRGPRRYRTPSRSRSRDRFRRSETPPHWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKEKKITDHRHMSESPNRKIEKEKKVKDHKSESKERDIRRNSEKDDKYNKNKVKKRGKSKSRSKSKERSKSKERDSKHSRHEDKRVRSRSKERDHETTKEKEKQLDSKGKDQERSRSKENSKQVESKSNEHDHSKSKEKDRRAQSRSRERDLTKSKHSYNSRTRERSRSRDRSRRVRSRSHDRDRSRSKEYHRYREQEYRRRGRSRSRDRRTPGRSRSKDRRRRRRDSRSSEREESQSRNKEKYRSQDSKSSHRKENSEGEKRMYSKSRDHSSSNNNREKKADIDQSPVSKTKQSSQDNEVKSSTLKNQEDEKTRSPVEKENQKSKGQENDHVHDKNKKCDHESSPGTDEDKSG
|
5.2.1.8
| null |
protein folding [GO:0006457]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]
|
PF00160;
|
2.40.100.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:9525923}. Nucleus speckle {ECO:0000269|PubMed:9525923}. Note=Colocalizes with splicing factors at nuclear speckles. {ECO:0000269|PubMed:9525923}.
|
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:9525923};
| null | null | null | null |
FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. {ECO:0000269|PubMed:9525923}.
|
Rattus norvegicus (Rat)
|
O55036
|
TERF1_CRIGR
|
MAEDVSSTAPSPRGCADGRDADPTEEQMAQTQRNDQDQFECQELLECQVQVGAPDEEEEEEEDSGLVAEAEAVAAGWMLHFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIKIPAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYYHMMEKIKSYVNYVLSEKSSTFLMKAAAKVVESKRTRTITSQDKPSGNDVEMETEANLDTRKSVSDKQSAVTESSEGTVSLLRSHKNLFLSKLQHGTQQQDLNKKERRVGTPQSTKKKKESRRATESRIPVSKSQPVTPEKHRARKRQAWLWEEDKNLRSGVRKYGEGNWSKILLHYKFNNRTSVMLKDRWRTMKKLKLISSDSE
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; negative regulation of DNA replication [GO:0008156]; negative regulation of telomeric D-loop disassembly [GO:1905839]; telomere maintenance via telomerase [GO:0007004]
|
cytoplasm [GO:0005737]; nuclear telomere cap complex [GO:0000783]; nucleus [GO:0005634]; spindle [GO:0005819]
|
ankyrin repeat binding [GO:0071532]; DNA binding, bending [GO:0008301]; double-stranded telomeric DNA binding [GO:0003691]; G-rich strand telomeric DNA binding [GO:0098505]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; telomerase activity [GO:0003720]
|
PF00249;PF08558;
|
1.10.10.60;1.25.40.210;
| null |
PTM: Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage. {ECO:0000250}.; PTM: ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA. {ECO:0000250}.; PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex, leading to its degradation by the proteasome (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}. Chromosome, telomere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle via its C-terminal domain (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways (By similarity). {ECO:0000250}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O55038
|
CXL13_MOUSE
|
MRLSTATLLLLLASCLSPGHGILEAHYTNLKCRCSGVISTVVGLNIIDRIQVTPPGNGCPKTEVVIWTKMKKVICVNPRAKWLQRLLRHVQSKSLSSTPQAPVSKRRAA
| null | null |
activation of GTPase activity [GO:0090630]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; B cell chemotaxis [GO:0035754]; B cell chemotaxis across high endothelial venule [GO:0035769]; cell-cell signaling [GO:0007267]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; defense response to bacterium [GO:0042742]; endothelial cell chemotaxis to fibroblast growth factor [GO:0035768]; inflammatory response [GO:0006954]; lymph node development [GO:0048535]; lymphocyte chemotaxis across high endothelial venule [GO:0002518]; neutrophil chemotaxis [GO:0030593]; positive regulation of cell-cell adhesion mediated by integrin [GO:0033634]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of integrin activation [GO:0033625]; positive regulation of T cell chemotaxis [GO:0010820]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
CCR10 chemokine receptor binding [GO:0031735]; chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; CXCR5 chemokine receptor binding [GO:0031724]; fibroblast growth factor binding [GO:0017134]; heparin binding [GO:0008201]; receptor ligand activity [GO:0048018]
|
PF00048;
|
2.40.50.40;
|
Intercrine alpha (chemokine CxC) family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Strongly chemotactic for B-lymphocytes, weakly for spleen monocytes and macrophages but no chemotactic activity for granulocytes. Binds to BLR1/CXCR5. May play a role in directing the migration of B-lymphocytes to follicles in secondary lymphoid organs.
|
Mus musculus (Mouse)
|
O55042
|
SYUA_MOUSE
|
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA
| null | null |
adult locomotory behavior [GO:0008344]; behavioral response to cocaine [GO:0048148]; cellular response to copper ion [GO:0071280]; cellular response to oxidative stress [GO:0034599]; chemical synaptic transmission [GO:0007268]; dopamine biosynthetic process [GO:0042416]; dopamine metabolic process [GO:0042417]; excitatory postsynaptic potential [GO:0060079]; fatty acid metabolic process [GO:0006631]; long-term synaptic potentiation [GO:0060291]; membrane organization [GO:0061024]; microglial cell activation [GO:0001774]; mitochondrial ATP synthesis coupled electron transport [GO:0042775]; mitochondrial membrane organization [GO:0007006]; negative regulation of chaperone-mediated autophagy [GO:1904715]; negative regulation of dopamine metabolic process [GO:0045963]; negative regulation of dopamine uptake involved in synaptic transmission [GO:0051585]; negative regulation of exocytosis [GO:0045920]; negative regulation of microtubule polymerization [GO:0031115]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of norepinephrine uptake [GO:0051622]; negative regulation of platelet-derived growth factor receptor signaling pathway [GO:0010642]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of serotonin uptake [GO:0051612]; negative regulation of thrombin-activated receptor signaling pathway [GO:0070495]; neuron apoptotic process [GO:0051402]; neurotransmitter secretion [GO:0007269]; neutral lipid metabolic process [GO:0006638]; phospholipid metabolic process [GO:0006644]; positive regulation of endocytosis [GO:0045807]; positive regulation of exocytosis [GO:0045921]; positive regulation of hydrogen peroxide catabolic process [GO:1903285]; positive regulation of inflammatory response [GO:0050729]; positive regulation of inositol phosphate biosynthetic process [GO:0060732]; positive regulation of neurotransmitter secretion [GO:0001956]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein localization to cell periphery [GO:1904377]; positive regulation of receptor recycling [GO:0001921]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of SNARE complex assembly [GO:0035543]; positive regulation of synaptic transmission [GO:0050806]; protein complex oligomerization [GO:0051259]; protein destabilization [GO:0031648]; protein tetramerization [GO:0051262]; receptor internalization [GO:0031623]; regulation of acyl-CoA biosynthetic process [GO:0050812]; regulation of dopamine secretion [GO:0014059]; regulation of glutamate secretion [GO:0014048]; regulation of locomotion [GO:0040012]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of macrophage activation [GO:0043030]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of neurotransmitter secretion [GO:0046928]; regulation of presynapse assembly [GO:1905606]; regulation of reactive oxygen species metabolic process [GO:2000377]; response to interleukin-1 [GO:0070555]; response to iron(II) ion [GO:0010040]; response to lipopolysaccharide [GO:0032496]; response to magnesium ion [GO:0032026]; response to type II interferon [GO:0034341]; response to xenobiotic stimulus [GO:0009410]; SNARE complex assembly [GO:0035493]; synapse organization [GO:0050808]; synaptic transmission, dopaminergic [GO:0001963]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle priming [GO:0016082]; synaptic vesicle transport [GO:0048489]
|
actin cytoskeleton [GO:0015629]; axon terminus [GO:0043679]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular space [GO:0005615]; growth cone [GO:0030426]; inclusion body [GO:0016234]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nuclear outer membrane [GO:0005640]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; platelet alpha granule membrane [GO:0031092]; postsynapse [GO:0098794]; presynapse [GO:0098793]; protein-containing complex [GO:0032991]; ribosome [GO:0005840]; supramolecular fiber [GO:0099512]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]
|
actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; arachidonic acid binding [GO:0050544]; beta-tubulin binding [GO:0048487]; calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; cuprous ion binding [GO:1903136]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; dynein complex binding [GO:0070840]; enzyme binding [GO:0019899]; ferrous iron binding [GO:0008198]; histone binding [GO:0042393]; Hsp70 protein binding [GO:0030544]; identical protein binding [GO:0042802]; kinesin binding [GO:0019894]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; oxidoreductase activity [GO:0016491]; phospholipase binding [GO:0043274]; phospholipid binding [GO:0005543]; phosphoprotein binding [GO:0051219]; protein domain specific binding [GO:0019904]; SNARE binding [GO:0000149]; tau protein binding [GO:0048156]; zinc ion binding [GO:0008270]
|
PF01387;
|
1.10.287.700;
|
Synuclein family
|
PTM: Phosphorylated, predominantly on serine residues. Phosphorylated on Tyr-125 upon osmotic stress. {ECO:0000250|UniProtKB:P37840}.; PTM: Ubiquitinated. The predominant conjugate is the diubiquitinated form. {ECO:0000250|UniProtKB:P37377}.; PTM: Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure. {ECO:0000250|UniProtKB:P37840}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31034892}. Membrane {ECO:0000250|UniProtKB:P37840}. Nucleus {ECO:0000250|UniProtKB:P37840}. Synapse {ECO:0000250|UniProtKB:P37840}. Secreted {ECO:0000250|UniProtKB:P37840}. Cell projection, axon {ECO:0000269|PubMed:17296554}. Note=Membrane-bound in dopaminergic neurons (By similarity). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (PubMed:17296554). {ECO:0000250|UniProtKB:P37840, ECO:0000269|PubMed:17296554}.
| null | null | null | null | null |
FUNCTION: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed:20798282, PubMed:25246573). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity). {ECO:0000250|UniProtKB:P37840, ECO:0000269|PubMed:20798282, ECO:0000269|PubMed:25246573}.
|
Mus musculus (Mouse)
|
O55043
|
ARHG7_RAT
|
MTDNANSQLVVRAKFNFQQTNEDELSFSKGDVIHVTRVEEGGWWEGTHNGRTGWFPSNYVREIKPSEKPVSPKSGTLKSPPKGFDTTAINKSYYNVVLQNILETEHEYSKELQSVLSTYLWPLQTSEKLSSANTSYLMGNLEEISSFQQVLVQSLEECTKSPEAQQRVGGCFLSLMPQMRTLYLAYCANHPSAVSVLTEHSEDLGEFMETKGASSPGILVLTTGLSKPFMRLDKYPTLLKELERHMEDYHPDRQDIQKSMTAFKNLSAQCQEVRKRKELELQILTEPIRSWEGDDIKTLGSVTYMSQVTIQCAGSEEKNERYLLLFPNLLLMLSASPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCNNQQDLHEWVEHLQRQTKVTSVSNPTIKPHSVPSHTLPSHPLTPSSKHADSKPVALTPAYHTLPHPSHHGTPHTTISWGPLEPPKTPKPWSLSCLRPAPPLRPSAALCYKEDLSRSPKTMKKLLPKRKPERKPSDEEFAVRKSTAALEEDAQILKVIEAYCTSAKTRQTLNSSSRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDNKKMKKSLEEEQRARKDLEKLVRKVLKNMNDPAWDETNL
| null | null |
astrocyte cell migration [GO:0043615]; Golgi organization [GO:0007030]; hematopoietic progenitor cell differentiation [GO:0002244]; lamellipodium assembly [GO:0030032]; negative regulation of microtubule nucleation [GO:1905833]; positive regulation of apoptotic process [GO:0043065]; positive regulation of growth hormone secretion [GO:0060124]; postsynaptic actin cytoskeleton organization [GO:0098974]; presynaptic actin cytoskeleton organization [GO:0099140]; Rho protein signal transduction [GO:0007266]; small GTPase-mediated signal transduction [GO:0007264]
|
cell cortex [GO:0005938]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; GABA-ergic synapse [GO:0098982]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; mitotic spindle pole [GO:0097431]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; protein-containing complex [GO:0032991]; ruffle [GO:0001726]; storage vacuole [GO:0000322]
|
gamma-tubulin binding [GO:0043015]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase binding [GO:0019901]
|
PF16523;PF00169;PF00621;PF16614;PF07653;
|
1.20.900.10;1.20.5.390;2.30.29.30;2.30.30.40;
| null |
PTM: Phosphorylated on Ser-516 by CaMK1; enhancement of GEF activity and downstream activation of RAC1. Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Detected at cell adhesions. A small proportion is detected at focal adhesions.
| null | null | null | null | null |
FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O55044
|
G6PD_CRIGR
|
MAEQVALSRTQVCGILREELYQGDAFHQADTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPEDTFIVGYARSRLTVDDIRKQSEPFFKATPEERPKLEEFFARNSYVAGQYDDPASYKHLNSHMNALHQGMQANRLFYLALPPTVYEAVTKNIQETCMSQTGWNRIIVEKPFGRDLQSSNQLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTDSDDVRDEKVKVLKCISEVETSNVVLGQYVGNPNGEGEATNGYLDDPTVPRGSTTATFAAAVLYVENERWDGVPFILRCGKALNERKAEVRLQFRDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHKIDQEKPQPIPYVYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL
|
1.1.1.49
| null |
cellular response to oxidative stress [GO:0034599]; cholesterol biosynthetic process [GO:0006695]; erythrocyte maturation [GO:0043249]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glutathione metabolic process [GO:0006749]; NADP metabolic process [GO:0006739]; negative regulation of protein glutathionylation [GO:0010734]; pentose biosynthetic process [GO:0019322]; pentose-phosphate shunt, oxidative branch [GO:0009051]; ribose phosphate biosynthetic process [GO:0046390]
|
centriolar satellite [GO:0034451]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]
|
glucose binding [GO:0005536]; glucose-6-phosphate dehydrogenase activity [GO:0004345]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]
|
PF02781;PF00479;
|
3.40.50.720;
|
Glucose-6-phosphate dehydrogenase family
|
PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity (By similarity). {ECO:0000250|UniProtKB:P11413}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11413}. Membrane {ECO:0000250|UniProtKB:P11413}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11413}.
|
CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842; Evidence={ECO:0000250|UniProtKB:P11413};
| null |
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000250|UniProtKB:P11413}.
| null | null |
FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes. {ECO:0000250|UniProtKB:P11413}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O55047
|
TLK2_MOUSE
|
MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYDTSQGKGTPRGHKISDYFERRAEQPLYGLDGSAAKEASEEQSALPTLMSVMLAKPRLDTEQLAPRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q86UE8};
|
cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; chromosome segregation [GO:0007059]; DNA damage response [GO:0006974]; intracellular signal transduction [GO:0035556]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; peptidyl-serine phosphorylation [GO:0018105]; protein phosphorylation [GO:0006468]; regulation of chromatin organization [GO:1902275]; spermatogenesis [GO:0007283]
|
intermediate filament [GO:0005882]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Phosphorylated at Ser-696, probably by CHEK1. {ECO:0000250}.; PTM: Autophosphorylated; phosphorylation promotes the assembly of higher order oligomers and enzymatic activity. {ECO:0000250|UniProtKB:Q86UE8}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10455159}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q86UE8}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10455159}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10455159}. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2. {ECO:0000269|PubMed:10455159}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q86UE8}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q86UE8};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (By similarity). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (By similarity). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (By similarity). Negative regulator of amino acid starvation-induced autophagy (By similarity). {ECO:0000250|UniProtKB:Q86UE8}.; FUNCTION: Testis-specific isoforms may play a role in spermatogenesis. Highly expressed in embryos throughout development. {ECO:0000269|PubMed:10092119}.
|
Mus musculus (Mouse)
|
O55055
|
TRDMT_MOUSE
|
MEPLRVLELYSGIGGMHHALRESHIPAHVVAAIDVNTVANEVYKHNFPHTHLLSKTIEGISLEDFDKLSFNMILMSPPCQPFTRIGLQGDMTDPRTTSFLYILDILPRLQKLPKYILLENVKGFEVSSTRGLLIQTIEACGFQYQEFLLSPSSLGIPNSRLRYFLIAKLQSEPFPFQAPGQILMEFPKIVTVEPQKYAVVEESQPRVQRTGPRICAESSSTQSSGKDTILFKLETVEERDRKHQQDSDLSVQMLKDFLEDGDTDEYLLPPKLLLRYALLLDIVKPTSRRSMCFTKGYGSYIEGTGSVLQAAEDAQIENIYKSLPDLPPEEKIAKLSMLKLRYFTPKEIANLQGFPPEFGFPEKTTVKQRYRLLGNSLNVHVVAKLLTVLCEGFGNASESCHKMPLILDSNSKILS
|
2.1.1.204
| null |
response to amphetamine [GO:0001975]; tRNA methylation [GO:0030488]; tRNA stabilization [GO:0036416]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
RNA binding [GO:0003723]; tRNA (cytidine-5-)-methyltransferase activity [GO:0016428]; tRNA methyltransferase activity [GO:0008175]
|
PF00145;
|
3.90.120.10;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14717}.
|
CATALYTIC ACTIVITY: Reaction=cytidine(38) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(38) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42956, Rhea:RHEA-COMP:10299, Rhea:RHEA-COMP:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.204; Evidence={ECO:0000269|PubMed:22885326}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42957; Evidence={ECO:0000269|PubMed:22885326};
| null | null | null | null |
FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp) (PubMed:21183079, PubMed:22885326, PubMed:26271101). Has higher activity on tRNA(Asp) modified with queuosine at position 34 (By similarity). {ECO:0000250|UniProtKB:O14717, ECO:0000269|PubMed:21183079, ECO:0000269|PubMed:22885326, ECO:0000269|PubMed:26271101}.
|
Mus musculus (Mouse)
|
O55058
|
FBLN4_CRIGR
|
MLPFASCLPGSLLLWALLLLLLGAASPQDSEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDEQESCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKVGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECSYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYVQVSDNRCFCPVSNPLCREQPSSIVHRYMSITSERSVPADVFQIQATSVYPGAYNAFQIRAGNTQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF
| null | null |
aorta development [GO:0035904]; aorta smooth muscle tissue morphogenesis [GO:0060414]; elastic fiber assembly [GO:0048251]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; positive regulation of aortic smooth muscle cell differentiation [GO:1904831]; positive regulation of collagen fibril organization [GO:1904028]; positive regulation of smooth muscle cell-matrix adhesion [GO:1905609]; regulation of collagen fibril organization [GO:1904026]; vascular associated smooth muscle cell development [GO:0097084]
|
basement membrane [GO:0005604]; elastic fiber [GO:0071953]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; microfibril [GO:0001527]
|
calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; protein homodimerization activity [GO:0042803]
|
PF12662;PF07645;PF12661;
|
2.10.25.10;
|
Fibulin family
|
PTM: N-glycosylated; contains mostly complex-type glycans. Not O-glycosylated. {ECO:0000250|UniProtKB:O95967}.; PTM: Cleaved by ELANE; produces a 50-55 kDa fragment. Cleaved by MMP2 and MMP9; produces several fragments. {ECO:0000250|UniProtKB:O95967}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9WVJ9}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9WVJ9}. Note=Localizes on the microfibrils surrounding ELN cores. {ECO:0000250|UniProtKB:Q9WVJ9}.
| null | null | null | null | null |
FUNCTION: Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta. In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin. Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction. Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling. {ECO:0000250|UniProtKB:Q9WVJ9}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O55070
|
DNSL3_MOUSE
|
MSLHPASPRLASLLLFILALHDTLALRLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSRRSTTYNYVISSRLGRNTYKEQYAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVKKSTSCAYDRIVLCGQEIVNSVVPRSSGVFDFQKAYDLSEEEALDVSDHFPVEFKLQSSRAFTNNRKSVSLKKRKKGNRS
|
3.1.21.-
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q13609}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13609};
|
apoptotic DNA fragmentation [GO:0006309]; DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; programmed cell death involved in cell development [GO:0010623]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:0070948]
|
endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; nucleus [GO:0005634]
|
deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]; DNA endonuclease activity [GO:0004520]; endonuclease activity [GO:0004519]
|
PF03372;
|
3.60.10.10;
|
DNase I family
|
PTM: Poly-ADP-ribosylated by PARP1. ADP-ribosylation negatively regulates enzymatic activity during apoptosis. {ECO:0000250|UniProtKB:Q13609}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13609, ECO:0000269|PubMed:12050166}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13609}. Secreted {ECO:0000269|PubMed:12095301, ECO:0000269|PubMed:15796714, ECO:0000269|PubMed:27293190}. Note=Contradictory reports exist about the subcellular localization under normal physiological conditions. Shown to translocate to rough endoplasmic reticulum and to be transported through the entire secretory pathway for secretion. However, under conditions of cell death, may diffuse and/or be actively transported to the nucleus. {ECO:0000305|PubMed:15796714, ECO:0000305|PubMed:27293190}.
| null | null | null | null | null |
FUNCTION: Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (By similarity). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA (PubMed:12095301, PubMed:15796714, PubMed:19154352). Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and necrosis. The role in apoptosis includes myogenic and neuronal differentiation, and BCR-mediated clonal deletion of self-reactive B cells (PubMed:12050166, PubMed:15167901, PubMed:17218958, PubMed:24312463). Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity (PubMed:15796714, PubMed:27293190). Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs) (PubMed:29191910). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (PubMed:29191910). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (PubMed:29191910). {ECO:0000250|UniProtKB:O89107, ECO:0000269|PubMed:12050166, ECO:0000269|PubMed:15167901, ECO:0000269|PubMed:17218958, ECO:0000269|PubMed:24312463, ECO:0000269|PubMed:27293190, ECO:0000269|PubMed:29191910, ECO:0000305|PubMed:15796714}.
|
Mus musculus (Mouse)
|
O55074
|
AKA7A_MOUSE
|
MGQLCCFPFARDEGKICEKDRREPEDAELVRLSKRLVENAVLKAVQQYLEETQNKKQPGEGNSTKAEEGDRNGDGSDNNRK
| null | null |
modulation of chemical synaptic transmission [GO:0050804]; protein localization [GO:0008104]; regulation of protein kinase A signaling [GO:0010738]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]
|
apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; exocytic vesicle [GO:0070382]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; lateral plasma membrane [GO:0016328]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; sarcoplasmic reticulum [GO:0016529]; T-tubule [GO:0030315]
|
AMP binding [GO:0016208]; protein domain specific binding [GO:0019904]; protein kinase A binding [GO:0051018]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]
|
PF10470;
| null | null | null |
SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000269|PubMed:9545239}.
| null | null | null | null | null |
FUNCTION: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). {ECO:0000250, ECO:0000269|PubMed:9620705}.
|
Mus musculus (Mouse)
|
O55075
|
CADH2_CRIGR
|
TKPLDRELIARFHLRAHAVDINGNRVENPIDIVINVIDMNDNRPEFLHQVWNGSVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVEVIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIHTDPNSNDGLVTVVKPIDFETNRMFV
| null | null |
adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; glial cell differentiation [GO:0010001]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neuronal stem cell population maintenance [GO:0097150]; regulation of axonogenesis [GO:0050770]; regulation of synaptic transmission, glutamatergic [GO:0051966]; synapse assembly [GO:0007416]
|
adherens junction [GO:0005912]; apical part of cell [GO:0045177]; catenin complex [GO:0016342]; cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; sarcolemma [GO:0042383]
|
cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]
|
PF00028;
|
2.60.40.60;
| null |
PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound C-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa. Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate neural stem cell quiescence (By similarity). {ECO:0000250}.; PTM: May be phosphorylated by OBSCN. {ECO:0000250|UniProtKB:P15116}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000250|UniProtKB:P19022}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {ECO:0000250|UniProtKB:P15116}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P15116}. Note=Colocalizes with TMEM65 at the intercalated disk in cardiomyocytes. Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes. {ECO:0000250|UniProtKB:P15116}.
| null | null | null | null | null |
FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density. {ECO:0000250|UniProtKB:P10288, ECO:0000250|UniProtKB:P15116}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O55076
|
CDK2_CRIGR
|
MENFQKVEKIGEGTYGVVYKAKNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASAVTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINAEGSIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
|
2.7.11.22
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P24941}; Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:P24941};
|
cell division [GO:0051301]; DNA repair [GO:0006281]; G1/S transition of mitotic cell cycle [GO:0000082]; meiotic cell cycle [GO:0051321]; protein phosphorylation [GO:0006468]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of gene expression [GO:0010468]; response to organic substance [GO:0010033]; signal transduction [GO:0007165]
|
Cajal body [GO:0015030]; centrosome [GO:0005813]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; endosome [GO:0005768]; midbody [GO:0030496]
|
ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein kinase activity [GO:0097472]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
|
PTM: Phosphorylated at Thr-160 by CDK7 in a CAK complex. Phosphorylation at Thr-160 promotes kinase activity, whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being dephosphorylated by CDC25A. {ECO:0000250|UniProtKB:P24941}.; PTM: Nitrosylated after treatment with nitric oxide (DETA-NO). {ECO:0000250|UniProtKB:P24941}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Note=Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the inhibition by 1,25-(OH)(2)D(3) (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000269|PubMed:11506705}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000269|PubMed:11506705};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis (PubMed:11506705). Phosphorylates CABLES1, CTNNB1, CDK2AP2, ERCC6, NBN, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in embryonic stem cells (ESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Involoved in regulation of telomere repar by mediating phosphorylation of NBN. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization (By similarity). Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (By similarity). {ECO:0000250|UniProtKB:P24941, ECO:0000250|UniProtKB:P97377, ECO:0000269|PubMed:11506705}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O55082
|
PTN20_MOUSE
|
MSSPRKVRGKTGRDNDEEEGNSGNLNLRNSLPSSSQKMTPTKPIFGNKMNSENVKPSHHLSFSDKYELVYPEPLESDTDETVWDVSDRSLRNRWNSMDSETAGPSKTVSPVLSGSSRLSKDTETSVSEKELTQLAQIRPLIFNSSARSAMRDCLNTLQKKEELDIIREFLELEQMTLPDDFNSGNTLQNRDKNRYRDILPYDSTRVPLGKNKDYINASYIRIVNHEEEYFYIATQGPLPETIEDFWQMVLENNCNVIAMITREIECGVIKCYSYWPISLKEPLEFEHFSVFLETFHVTQYFTVRVFQIVKKSTGKSQCVKHLQFTKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICVDVVFSAIEKNYSFDIMNIVTQMRKQRCGMIQTKEQYQFCYEIVLEVLQNLLALY
|
3.1.3.48
| null |
dephosphorylation [GO:0016311]
|
centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; microtubule [GO:0005874]; nucleus [GO:0005634]
|
phosphoprotein phosphatase activity [GO:0004721]
|
PF00102;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family, Non-receptor class subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with the microtubule-organizing center and intracellular membrane compartments. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:9407093};
| null | null | null | null |
FUNCTION: Tyrosine-protein phosphatase targeted to sites of actin polymerization in response of varied extracellular stimuli. Has tyrosine phosphatase activity towards various tyrosyl phosphorylated substrates.
|
Mus musculus (Mouse)
|
O55087
|
MEF2B_MOUSE
|
MGRKKIQISRILDQRNRQVTFTKRKFGLMKKAYELSVLCDCDIALIIFNSAQRLFQYASSDMDRVLLKYTEYSEPHESRTNADILQTLKRRGVGLDGPELDMEEGPEGPGEKLLRTLGGDRGSASPRPRIYPVAPAMSVSELSYRVPPATPGCDPGGLGEVPSVHSRPAYFRPPGLGHPIFSPSHLASKTPPPLYLATDGRRPDLPPGLVGARGGLGTSRSLYSGLQSPGAPGPALGSFAFLPSGSTDCSPGDAAQGPLQPSPWPPTRDAVDPARPVARSLCKEGPPSRGASPPTPPVSIKSERLSPVTGTSGDFPRSFPYPLLLARPLAEPLRPSASLHRLTPDSWPR
| null | null |
cell differentiation [GO:0030154]; heart development [GO:0007507]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]
|
nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone deacetylase binding [GO:0042826]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00319;
|
3.40.1810.10;
|
MEF2 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription. {ECO:0000269|PubMed:8668199, ECO:0000269|PubMed:9443808}.
|
Mus musculus (Mouse)
|
O55091
|
IMPCT_MOUSE
|
MAEEEVGNSQRQSEEIEAMAAIYGEEWCVIDENAKIFCIRVTDFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIYVHNMGESILYQWVEKIRDALIQKSQITEPDPDVKKKTEEVEVESEEDPILEHPPENPVKTLDLKISEETQPETEELPPVAHGVPITDRRSTFQAHVAPVVCPEQVKLVLAKLYENKKIASATHNIYAYRIFCEDKQTFLQDCEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNFTNTPDESTKNLGKKKVKKDKKKNDH
| null | null |
cellular response to amino acid starvation [GO:0034198]; GCN2-mediated signaling [GO:0140469]; intracellular signal transduction [GO:0035556]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron projection extension [GO:1990138]; positive regulation of neuron differentiation [GO:0045666]; regulation of cytoplasmic translational initiation in response to stress [GO:1990611]; regulation of translational initiation [GO:0006446]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
actin binding [GO:0003779]; protein sequestering activity [GO:0140311]; ribosome binding [GO:0043022]
|
PF05773;PF01205;
|
3.30.230.30;3.10.110.10;
|
IMPACT family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23447528}.
| null | null | null | null | null |
FUNCTION: Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis (PubMed:15937339, PubMed:23447528, PubMed:24333428). May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis (PubMed:15937339, PubMed:23447528). Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth (PubMed:23447528). {ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:23447528, ECO:0000269|PubMed:24333428}.
|
Mus musculus (Mouse)
|
O55092
|
SLK_CAVPO
|
MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWETIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLKKCLEKNVDARWTTSQLLQHPFVTIDSNKPIRELIAEAKAEVTEEVEDGKEEDDDEEIENSLPIPTNKRASSDLSIASSEEDKLSQNACILESVSEKTEHNASGDKFSTKVLNEKPCPGEPENAVELVGGAVAVLPDRATELPESGREEKRPKLDRLPDTEDQEMADINSVSEGEEDHAVTSETNIEHNLKPEKERDQEKQPVLENKLVKSEDTTIQTVDLVSQETGEKEVDIHILDSEVVHAVEDTHEKLRKDDTTQKDVISDTSSVGERDEEIGAVPKTAESSAEGAQGDGGKETDEGAQILISKATEGPKASGTEEAPPVTEITETNDTDQKLVENTHEKQLPISSETTLDTSEGLGASEGREVTESGSTEEVEVEGAVSETDEEDVQSETRGAPMAVTQMDTEKNETPHEAPAQVEVQVPVPPQPSEPPPAPIPSININSEAAENKGEMGASLNTETILLPESESQKENDTDSGTGSTADNSSIDLNLSISSFLSKTKDNGSISLQETRRQKKTLKKTRKFIVDGVEVSVTTSKIVTDSDSKTEELRFLRRQELRELRFLQKEEQRAQQQLNGKLQQQREQIFRRFEQEMMSKKRQYDQEIENLEKQQKQTIERLEQEHTNRLRDEAKRIKGEQEKELSKFQNILKNRKKEVLNEVEKAPKDLRKELMKRRKEELAQSQHVQEQDFVQKQQQELDGSLKKIIQQQKAELANIERECLNNKQQLMRAREAAIWELEERHLQEKHQLLKQQLKDQYFMQRHQLLKRHEKETEQMQRYNQRLIEELKNRQTQERARLPKIQRSEAKTRMAMFKKSLRINSTATPDQDRDKIKQFSAQEEKRQKNERMAQHQKHENQMRDLQLQCEANVRELHQLQNEKCHLLVEHETQKLKELDEEHSQELKEWREKLRPRKKTLEEEFARKLQEQEVFFKMTGESECLNPSTQSRISKFYPIPSLHSTGS
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; protein autophosphorylation [GO:0046777]; regulation of cell migration [GO:0030334]; regulation of focal adhesion assembly [GO:0051893]
|
cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
|
ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF12474;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}.; PTM: Autophosphorylated. {ECO:0000269|PubMed:9143322}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Mediates apoptosis and actin stress fiber dissolution. {ECO:0000250}.
|
Cavia porcellus (Guinea pig)
|
O55096
|
DPP3_RAT
|
MADTQYILPNDIGVSSLDCREAFRLLSPTERLYAHHLSRAAWYGGLAVLLQTSPEAPYIYALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPKEKLERVILGSKAAQQHPEEVRSLWQTCGELMFSLEPRLRHLGLGKEGVTTYFSGDCAMEDAKLAQDFLDSQNLSAYNTRLFKVVGQEGKYHYEVRLASVLNTEPALDSELTSKLKSYEFQGNHFQVTRGDYAPILQKVVEHLEKAKAYAANSHQEQMLAQYVESFTQGSIEAHKRGSRFWIQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAMVNKDMSAKFERLVASAEQLLKELPWPPAFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYATKREKLTFMEEEDKDLYIRWKGPSFDVQVGLHELLGHGSGKLFVQDEKGAFNFDQETVINPETGEQIQSWYRSGETWDSKFSTIASSYEECRAESVGLYLCLNPQVLQIFGFEGTDAEDVIYVNWLNMVRAGLLALEFYTPETANWRQAHMQARFVILRVLLEAGEGLVTVTPTTGSDGRPDARVHLDRSKIRSVGKPALERFLRRLQVLKSTGDVVAGRALYEGYAAVTDAPPECFLTLRDTVLLRKESRKLIVQPNTRLEGSEVQLVEYEASAAGLIRSFCERFPEDGPELEEVLTQLATADAQFWRDQVQEAPSGQA
|
3.4.14.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10387075}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10387075};
|
protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
aminopeptidase activity [GO:0004177]; dipeptidyl-peptidase activity [GO:0008239]; metalloexopeptidase activity [GO:0008235]; zinc ion binding [GO:0008270]
|
PF03571;
|
3.30.540.30;
|
Peptidase M49 family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.; EC=3.4.14.4;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0.;
| null |
FUNCTION: Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin (By similarity). Also cleaves Arg-Arg-beta-naphthylamide. {ECO:0000250|UniProtKB:Q9NY33}.
|
Rattus norvegicus (Rat)
|
O55098
|
STK10_MOUSE
|
MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNDVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYYDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHGKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVLCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLQHPFVSRVTSNKALRELVAEAKAEVMEEIEDGREDGEEEDAVDAVPPLVNHTQDSANVTQPSLDSNKLLQDSSTPLPPSQPQEPVSGSCSQPSGDGPLQTTSPADGLSKNDNDLKVPVPLRKSRPLSMDARIQMDEEKQIPDQDENPSPAASKSQKANQSRPNSSALETLGGEALTNGGLELPSSVTPSHSKRASDCSNLSTSESMDYGTSLSADLSLNKETGSLSLKGSKLHNKTLKRTRRFVVDGVEVSITTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQTQLSSKHELQLEQMHKRFEQEINAKKKFYDVELENLERQQKQQVEKMEQDHSVRRKEEAKRIRLEQDRDYAKFQEQLKQMKKEVKSEVEKLPRQQRKESMKQKMEEHSQKKQRLDRDFVAKQKEDLELAMRKLTTENRREICDKERDCLSKKQELLRDREAALWEMEEHQLQERHQLVKQQLKDQYFLQRHDLLRKHEKEREQMQRYNQRMMEQLKVRQQQEKARLPKIQRSDGKTRMAMYKKSLHINGAGSASEQREKIKQFSQQEEKRQKAERLQQQQKHENQMRDMVAQCESNMSELQQLQNEKCHLLVEHETQKLKALDESHNQSLKEWRDKLRPRKKALEEDLNQKKREQEMFFKLSEEAEPRPTTPSKASNFFPYSSGDAS
|
2.7.11.1
| null |
cell cycle [GO:0007049]; lymphocyte aggregation [GO:0071593]; protein autophosphorylation [GO:0046777]; regulation of lymphocyte migration [GO:2000401]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF12474;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Autophosphorylates following homodimerization, leading to activation of the protein. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269|PubMed:19255442}.
|
Mus musculus (Mouse)
|
O55099
|
AURKB_RAT
|
MAQKENVYPWPYGSKTSQSGLNTLPQRVLRKEPAVTPAQALMNRSNSQSTAVPGQKLTENKGATALQGSQSRQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSGTFDEQRTATIMEELSDALMYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSMPLGAKDLISKLLKHNPSQRLPLEQVSAHPWVRANSRRVLPPSAL
|
2.7.11.1
| null |
abscission [GO:0009838]; cell cycle G2/M phase transition [GO:0044839]; cellular response to UV [GO:0034644]; cleavage furrow formation [GO:0036089]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic spindle midzone assembly [GO:0051256]; mitotic spindle organization [GO:0007052]; negative regulation of B cell apoptotic process [GO:0002903]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of cytokinesis [GO:0032466]; negative regulation of innate immune response [GO:0045824]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cytokinesis [GO:0032467]; positive regulation of lateral attachment of mitotic spindle microtubules to kinetochore [GO:1905116]; positive regulation of mitotic sister chromatid segregation [GO:0062033]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; post-translational protein modification [GO:0043687]; protein localization to kinetochore [GO:0034501]; protein phosphorylation [GO:0006468]; regulation of cytokinesis [GO:0032465]; spindle organization [GO:0007051]
|
chromocenter [GO:0010369]; chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole [GO:0097431]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [GO:0031616]
|
ATP binding [GO:0005524]; histone H3S28 kinase activity [GO:0044022]; kinase binding [GO:0019900]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
|
PTM: The phosphorylation of Thr-235 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-235 phosphorylation is indispensable for the AURKB kinase activity. {ECO:0000250|UniProtKB:Q96GD4}.; PTM: Acetylated at Lys-218 by KAT5 at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis. {ECO:0000250|UniProtKB:Q96GD4}.; PTM: Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, ubiquitination leads to removal from mitotic chromosomes and is required for cytokinesis. During anaphase, the BCR(KLHL21) E3 ubiquitin ligase complex recruits the CPC complex from chromosomes to the spindle midzone and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome. Deubiquitinated by USP35; inhibiting CDH1-mediated degradation of AURKB. {ECO:0000250|UniProtKB:Q96GD4}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GD4}. Chromosome {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96GD4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96GD4}. Midbody {ECO:0000250|UniProtKB:Q96GD4}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalized with gamma tubulin in the midbody. Proper localization of the active, Thr-235-phosphorylated form during metaphase may be dependent upon interaction with SPDYC. Colocalized with SIRT2 during cytokinesis with the midbody. Localization (and probably targeting of the CPC) to the inner centromere occurs predominantly in regions with overlapping mitosis-specific histone phosphorylations H3pT3 and H2ApT12. {ECO:0000250|UniProtKB:Q96GD4}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q96GD4}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q96GD4};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (By similarity). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (By similarity). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis (PubMed:9450992). Required for central/midzone spindle assembly and cleavage furrow formation (By similarity). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (By similarity). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP (By similarity). Phosphorylation of INCENP leads to increased AURKB activity (By similarity). Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone H3 (By similarity). A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres (By similarity). Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively) (By similarity). AURKB is also required for kinetochore localization of BUB1 and SGO1 (By similarity). Phosphorylation of p53/TP53 negatively regulates its transcriptional activity (By similarity). Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (By similarity). Acts as an inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the G2-M transition, blocking CGAS liquid phase separation and activation, and thereby preventing CGAS-induced autoimmunity (By similarity). Phosphorylates KRT5 during anaphase and telophase (By similarity). Phosphorylates ATXN10 which promotes phosphorylation of ATXN10 by PLK1 and may play a role in the regulation of cytokinesis and stimulating the proteasomal degradation of ATXN10 (By similarity). {ECO:0000250|UniProtKB:O70126, ECO:0000250|UniProtKB:Q96GD4, ECO:0000269|PubMed:9450992}.
|
Rattus norvegicus (Rat)
|
O55100
|
SNG1_MOUSE
|
MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWVFSIVVFGSIVNEGYLNNPEEEEEFCIYNRNPNACSYGVTVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFFWFVGFCFLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPSAGSDPAGMGGTYQHPANAFDAEPQGYQSQGY
| null | null |
cellular response to leukemia inhibitory factor [GO:1990830]; protein targeting [GO:0006605]; regulated exocytosis [GO:0045055]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of short-term neuronal synaptic plasticity [GO:0048172]; synaptic vesicle membrane organization [GO:0048499]
|
melanosome [GO:0042470]; neuromuscular junction [GO:0031594]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
| null |
PF01284;
| null |
Synaptogyrin family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62876}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62876}. Melanosome {ECO:0000250|UniProtKB:O43759}.
| null | null | null | null | null |
FUNCTION: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity (PubMed:10595519). {ECO:0000250|UniProtKB:Q62876, ECO:0000269|PubMed:10595519}.
|
Mus musculus (Mouse)
|
O55102
|
BL1S1_MOUSE
|
MLSRLLKEHQAKQNERKELQEKRRREAIAAATCLTEALVDHLNVGVAQAYMNQRKLDHEVKTLQVQAAQFAKQTGQWIGMVENFNQALKEIGDVENWARSIELDMRTIATALEYVYKGQLQSAPS
| null | null |
aerobic respiration [GO:0009060]; anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; endosomal transport [GO:0016197]; lysosome localization [GO:0032418]; melanosome organization [GO:0032438]; neuron projection development [GO:0031175]; organelle transport along microtubule [GO:0072384]; peptidyl-lysine acetylation [GO:0018394]; regulation of endosome size [GO:0051036]; regulation of lysosome size [GO:0062196]
|
axon cytoplasm [GO:1904115]; BLOC-1 complex [GO:0031083]; BORC complex [GO:0099078]; cytoplasmic side of lysosomal membrane [GO:0098574]; cytosol [GO:0005829]; early endosome [GO:0005769]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
| null |
PF06320;
| null |
BLOC1S1 family
| null |
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:22309213}. Mitochondrion matrix {ECO:0000269|PubMed:22309213}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78537}. Lysosome membrane {ECO:0000250|UniProtKB:P78537}.
| null | null | null | null | null |
FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension (PubMed:16760431, PubMed:19546860, PubMed:21998198). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. The BORC complex is most probably associated with the cytosolic face of lysosomes, may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity). {ECO:0000250|UniProtKB:P78537, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}.; FUNCTION: May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. May counteract the action of the deacetylase SIRT3 by acetylating and regulating proteins of the mitochondrial respiratory chain including ATP5F1A and NDUFA9. {ECO:0000250|UniProtKB:P78537}.
|
Mus musculus (Mouse)
|
O55103
|
PRAX_MOUSE
|
MEARSRSAEELRRAELVEIIVETEAQTGVSGFNVAGGGKEGIFVRELREDSPAAKSLSLQEGDQLLSARVFFENFKYEDALRLLQCAEPYKVSFCLKRTVPTGDLALRPGTVSGYEMKGPRAKVAKLNIQSLAPVKKKKMVTGALGTPADLAPVDVEFSFPKFSRLRRGLKAEAVKGPVPAAPARRRLQLPRLRVREVAEEAQVARMAAAAPPPRKAKAEAEAATGAGFTAPQIELVGPRLPSAEVGVPQVSVPKGTPSTEAASGFALHLPTLGLGAPAAPAVEPPATGIQVPQVELPTLPSLPTLPTLPCLDTQEGAAVVKVPTLDVAAPSMGVDLALPGAEVEAQGEVPEVALKMPRLSFPRFGIRGKEATEAKVVKGSPEAKAKGPRLRMPTFGLSLLEPRPSGPEAVAESKLKLPTLKMPSFGIGVAGPEVKAPTGPEVKLPKVPEVKLPKVPEAAIPDVQLPEVQLPKMSDMKLPKIPEMVVPDVRLPEVQLPKVPEMKVPEMKLPKWPEMAVPDVHLPDVQLPKVPEMKLPKVPEMAVPDVHLPDVQLPKVPEMKLPEMKLPKVPEMAVPDVRLPEVQLPKVSEVKLPKMPEMAVPDVHLPELQLPKMSEVKLPKMPEMAVPDVRLPEVQLPKVSEMKLPKMPEMTMPDIRLPEVQLPKVPDIKLPEMKLPEIKLPKVPDMAVPDVPLPELQLPKVSDIRLPEMQVSQVPEVQLPKMPEMKLSKVPEVQRKSAGAEQAKGTEFSFKLPKMTMPKLGKVGKPGEASIEVPDKLMTLPCLQPEVGTEASHVGVPSLSLPSVELDLPGALGLEGQVQEAVPGKVEKPEGPRVAVGVGEVGFRVPSVEIVTPQLPTVEVEKEQLEMVEMKVKPSSKFSLPKFGLSGPKAVKGEVEGPGRATKLKVSKFTISLPKARAGTEAEAKGAGEAGLLPALDLSIPQLSLDAQLPSGKVEVADSKPKSSRFALPKFGVKGRDSEADVLVAGEAELEGKGWGWDGKVKMPKLKMPSFGLSRGKEAETQDGRVSPGEKLEAIAGQLKIPAVELVTPGAQETEKVTSGVKPSGLQVSTTGQVVAEGQESVQRVSTLGISLPQVELASFGEAGPEIVAPSAEGTAGSRVQVPQVMLELPGTQVAGGDLLVGEGIFKMPTVTVPQLELDVGLGHEAQAGEAAKSEGGIKLKLPTLGTGSRGEGVEPQGPEAQRTFHLSLPDVELTSPVSSHAEYQVVEGDGDGGHKLKVRLPLFGLAKAKEGIEVGEKVKSPKLRLPRVGFSQSESVSGEGSPSPEEEEEGSGEGASSRRGRVRVRLPRVGLASPSKVSKGQEGDATSKSPVGEKSPKFRFPRVSLSPKARSGSRDREEGGFRVRLPSVGFSETAVPGSTRIEGTQAAAI
| null | null |
peripheral nervous system myelin formation [GO:0032290]; peripheral nervous system myelin maintenance [GO:0032287]; regulation of RNA splicing [GO:0043484]; sensory perception of pain [GO:0019233]; transmission of nerve impulse [GO:0019226]
|
anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
| null |
PF00595;
|
2.30.42.10;
|
Periaxin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21745462}. Cell junction {ECO:0000269|PubMed:21745462}. Note=Colocalizes with ACTB at tricellular junctions between eye lens fiber cells. {ECO:0000269|PubMed:21745462}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:9488714}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10671475}. Cytoplasm {ECO:0000250|UniProtKB:Q9BXM0}. Note=Detected in the Schwann cell nucleus prior to the onset of myelination (PubMed:10671475). Detected in Schwann cells at periaxonal myelin membranes. Associated with the cell membrane during myelination (PubMed:9488714). {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:9488714}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:9488714}.
| null | null | null | null | null |
FUNCTION: Scaffolding protein that functions as part of a dystroglycan complex in Schwann cells, and as part of EZR and AHNAK-containing complexes in eye lens fiber cells (PubMed:11430802, PubMed:21745462, PubMed:22764250). Required for the maintenance of the peripheral myelin sheath that is essential for normal transmission of nerve impulses and normal perception of sensory stimuli (PubMed:10839370). Required for normal transport of MBP mRNA from the perinuclear to the paranodal regions (PubMed:15356632). Required for normal remyelination after nerve injury (PubMed:10839370). Required for normal elongation of Schwann cells and normal length of the internodes between the nodes of Ranvier. The demyelinated nodes of Ranvier permit saltatory transmission of nerve impulses; shorter internodes cause slower transmission of nerve impulses (PubMed:15356632, PubMed:23022068). Required for the formation of appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane; the Schwann cell cytoplasm is restricted to regions between these appositions (PubMed:15356632, PubMed:23022068). Required for the formation of Cajal bands and of Schmidt-Lanterman incisures that correspond to short, cytoplasm-filled regions on myelinated nerves (PubMed:22764250, PubMed:23022068). Recruits DRP2 to the Schwann cell plasma membrane (PubMed:11430802, PubMed:22764250, PubMed:23022068). Required for normal protein composition of the eye lens fiber cell plasma membrane and normal eye lens fiber cell morphology (PubMed:21745462). {ECO:0000269|PubMed:10839370, ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:15356632, ECO:0000269|PubMed:22764250, ECO:0000269|PubMed:23022068}.
|
Mus musculus (Mouse)
|
O55111
|
DSG2_MOUSE
|
MARSPGDRCALLLLVQLLAVVCLDFGNGLHLEVFSPRNEGKPFPKHTHLVRQKRAWITAPVALREGEDLSRKNPIAKIHSDLAEEKGIKITYKYTGKGITEPPFGIFVFDRNTGELNITSILDREETPYFLLTGYALDSRGNNLEKPLELRIKVLDINDNEPVFTQEVFVGSIEELSAAHTLVMKITATDADDPETLNAKVSYRIVSQEPANSHMFYLNKDTGEIYTTSFTLDREEHSSYSLTVEARDGNGQITDKPVQQAQVQIRILDVNDNIPVVENKMYEGTVEENQVNVEVMRIKVTDADEVGSDNWLANFTFASGNEGGYFHIETDTQTNEGIVTLVKEVDYEEMKKLDLSIIVTNKAAFHKSILSKYKATPIPITVKVKNVVEGIHFKSSVVSFRASEAMDRSSLSRSIGNFQVFDEDTGQAAKVTYVKVQDTDNWVSVDSVTSEIKLVKIPDFESRYVQNGTYTAKVVAISKEHPQKTITGTIVITVEDVNDNCPVLVDSVRSVCEDEPYVNVTAEDLDGAQNSAPFSFSIIDQPPGTAQKWKITHQESTSVLLQQSERKRGRSEIPFLISDSQGFSCPERQVLQLTVCECLKGGGCVAAQYDNYVGLGPAAIALMILALLLLLLVPLLLLICHCGGGAKGFTPIPGTIEMLHPWNNEGAPPEDKVVPSLLVADHAESSAVRGGVGGAMLKEGMMKGSSSASVTKGQHELSEVDGRWEEHRSLLTAGATHHVRTAGTIAANEAVRTRATGSSRDMSGARGAVAVNEEFLRSYFTEKAASYNGEDDLHMAKDCLLVYSQEDTASLRGSVGCCSFIEGELDDLFLDDLGLKFKTLAEVCLGRKIDLDVDIEQRQKPVREASVSAASGSHYEQAVTSSESAYSSNTGFPAPKPLHEVHTEKVTQEIVTESSVSSRQSQKVVPPPDPVASGNIIVTETSYAKGSAVPPSTVLLAPRQPQSLIVTERVYAPTSTLVDQHYANEEKVLVTERVIQPNGGIPKPLEVTQHLKDAQYVMVRERESILAPSSGVQPTLAMPSVAAGGQNVTVTERILTPASTLQSSYQIPSETSITARNTVLSSVGSIGPLPNLDLEESDRPNSTITTSSTRVTKHSTMQHSYS
| null | null |
bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell-cell adhesion [GO:0098609]; desmosome organization [GO:0002934]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; maternal process involved in female pregnancy [GO:0060135]; Purkinje myocyte development [GO:0003165]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; response to progesterone [GO:0032570]
|
apical plasma membrane [GO:0016324]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; intracellular membrane-bounded organelle [GO:0043231]; lateral plasma membrane [GO:0016328]
|
calcium ion binding [GO:0005509]; cell adhesion molecule binding [GO:0050839]
|
PF00028;
|
2.60.40.60;4.10.900.10;
| null |
PTM: Palmitoylated by ZDHHC5 at the plasma membrane. {ECO:0000250|UniProtKB:Q14126}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14126}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14126}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q14126}.
| null | null | null | null | null |
FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
|
Mus musculus (Mouse)
|
O55112
|
AFF2_MOUSE
|
MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEEDLFSSGFDLFGEPYKVAEYTNKGDALANRVQNTLGSYDEMKDLLSNHSSQNHLVGIPKNSAPQTPISKSEASFYPEQKNRMIPSHQETTHSSTPMPPPSVVILNSTLIHSNRKSKSEWPRDSHNTSPAQASQTSSQPNKMQTSTQDPPQTRLEDFFVYPAEQPQIGTVEKSNPSSKEENNPNSGGEDTFKEIFQSNSPEESEFTVQAPGSPLVASSLLAPSSGLSVPTFPPGLYCKTSMGQQKPTAYVRPMDGQDQATDISPTLKPSIEFENSFGNLSFGSLLDGKPSAVSSKTKLPKFTILQTSEVSLTSDPSCVEEILRESQHLTPGFTLQKWSDPSSRASTKMLEDDLKLSSDEDDLEPVKTLTTQCTANELYQAVEKAKPKNNPVNPLLATPQSTPATQTNVGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDKWLNKVTSQNKSFICGQNETPTETISLPPPIIQPVEVQVKVKPNPSQAVAVPKERPLLSLIREKARPRPTQKTPETKALKHKLSTSVDTVSQRTIGKKQPKKVEKNTSFEEFTWPKPNITNSTPKEKGSVELPDPPRSRNKATAHKPVPRKEPRPHVPLATEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQIKVLPPCITSKSKETSNASLTLSTLTNGNSNNLSTSNEETAFSPPPAMQTELLSPLRDHENPKNLWVKIDLDLLSRVPGQNSVPVTPAKTDYKETASKPKRQTAATAVEKPAPKGKRKHKPAETAEKIPEKKQRLEDNTTICLLPPCISPAPPHKPPSTRENSSRRANRKKEEKLFPPALSPLAEDPPRRRNVSGNNGHFGQDKNISMAGQITSSKPKRSEGKFCATFKGISINEGDAPKKAASATVTVANMALATATATATVPAIVTATVTATATTTATATTTTTTTTISSITPTITSGLMDSSHLEMTSWAALPLLSSSSANVRRPKLTFDDSVHNADFYMQEAKKLKHKADALFEKFGKAVNYADAALSFTECGNAMERDPLEAKSPYTMYSETVELLRYAMRLKNFASPLASDGDKKLAVLCYRCLSLLYLRMFKLKKDHAMKYSRSLMEYFKQNASKVTQIPSPWVGNGKNTPSPVSLNNVSPINSVGNCNNGPVTIPQRIHHMAASHVNITSNVLRGYEHWDMADKLTRDNKEFFGDLDTLMGPLTQHSSMTNLVRYVRQGLCWLRIDAHLL
| null | null |
learning or memory [GO:0007611]; mRNA processing [GO:0006397]; negative regulation of gene expression [GO:0010629]; nuclear speck organization [GO:0035063]; regulation of gene expression [GO:0010468]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]
|
nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
G-quadruplex RNA binding [GO:0002151]
|
PF05110;PF18875;PF18876;
|
6.10.250.2670;
|
AF4 family
| null |
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19136466}. Note=When splicing or transcription are inhibited, accumulates in large, rounded speckles and in the nucleolus. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure. {ECO:0000269|PubMed:19136466}.
|
Mus musculus (Mouse)
|
O55123
|
MMP10_MOUSE
|
MEPLAILALLSLPICSAYPLHGAVTQGHPSMDLAQQYLEKYYNFKKNEKQIFKRKDSSPVVKKIQEMQKFLGLEMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFYPFDGPGQSLAHAYPPGPGFYGDVHFDDDEKWTLAPSGTNLFLVAAHELGHSLGLFHSDKKESLMYPVYRFSTSPANFHLSQDDIEGIQSLYGAGPSSDATVVPVLSVSPRPETPDKCDPALSFDSVSTLRGEVLFFKDRYFWRRSHWNPEPEFHLISAFWPTLPSDLDAAYEAHNTDSVLIFKGSQFWAVRGNEVQAGYPKGIHTLGFPPTVKKIDAAVFEKEKKKTYFFVGDKYWRFDETRHVMDKGFPRQITDDFPGIEPQVDAVLHEFGFFYFFRGSSQFEFDPNARTVTHILKSNSWLLC
|
3.4.24.22
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
|
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; regulation of cell migration [GO:0030334]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF00045;PF00413;PF01471;
|
3.40.390.10;2.110.10.10;
|
Peptidase M10A family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Similar to stromelysin 1, but action on collagen types III, IV and V is weak.; EC=3.4.24.22;
| null | null | null | null |
FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
|
Mus musculus (Mouse)
|
O55127
|
CP26A_MOUSE
|
MGLPALLASALCTFVLPLLLFLAALKLWDLYCVSSRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGAGCLSNLHDSSHKQRKKVIMQAFSREALQCYVLVIAEEVSSCLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPGPAGGGEDEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGVKARNLIHARIEENIRAKIRRLQATEPDGGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREEIKSKGLLCKSNQDNKLDMETLEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFTNKEEFNPDRFIVPHPEDASRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPARFTYFQGDI
|
1.14.13.-
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
anterior/posterior pattern specification [GO:0009952]; cellular response to retinoic acid [GO:0071300]; central nervous system development [GO:0007417]; neural crest cell development [GO:0014032]; retinoic acid catabolic process [GO:0034653]; retinoic acid metabolic process [GO:0042573]; retinoic acid receptor signaling pathway [GO:0048384]; sterol metabolic process [GO:0016125]; xenobiotic metabolic process [GO:0006805]
|
endoplasmic reticulum membrane [GO:0005789]
|
all-trans retinoic acid 18-hydroxylase activity [GO:0062183]; all-trans retinoic acid 4-hydrolase activity [GO:0062182]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; retinoic acid 4-hydroxylase activity [GO:0008401]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein. Microsome membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S)-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51492, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134185; Evidence={ECO:0000269|PubMed:9250660, ECO:0000269|PubMed:9442090, ECO:0000305|PubMed:15911617}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51493; Evidence={ECO:0000305|PubMed:15911617, ECO:0000305|PubMed:9250660, ECO:0000305|PubMed:9442090}; CATALYTIC ACTIVITY: Reaction=all-trans-(4S)-hydroxyretinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S,16)-dihydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51632, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134185, ChEBI:CHEBI:134233; Evidence={ECO:0000250|UniProtKB:O43174}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51633; Evidence={ECO:0000250|UniProtKB:O43174}; CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-18-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:139258; Evidence={ECO:0000269|PubMed:9442090, ECO:0000305|PubMed:15911617}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55857; Evidence={ECO:0000305|PubMed:15911617, ECO:0000305|PubMed:9442090};
| null | null | null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:15911617, PubMed:9250660, PubMed:9442090). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (PubMed:15911617, PubMed:9250660, PubMed:9442090). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity). Involved in the convertion of atRA to all-trans-4-oxo-RA (PubMed:15911617). Able to metabolize other RAs such as 9-cis, 13-cis and 9,13-di-cis RA (PubMed:9250660). Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (Probable). May play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid (By similarity). {ECO:0000250|UniProtKB:O43174, ECO:0000269|PubMed:15911617, ECO:0000269|PubMed:9250660, ECO:0000269|PubMed:9442090, ECO:0000305|PubMed:15911617}.
|
Mus musculus (Mouse)
|
O55128
|
SAP18_MOUSE
|
MAVESRVTQEEIKKEPEKPIDREKTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFMDLKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPSSGRMRPY
| null | null |
mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of apoptotic process [GO:0043065]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of DNA-templated transcription [GO:0006355]; RNA splicing [GO:0008380]
|
ASAP complex [GO:0061574]; cytoplasm [GO:0005737]; histone deacetylase complex [GO:0000118]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
transcription corepressor activity [GO:0003714]
|
PF06487;
|
3.10.20.550;
|
SAP18 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00422}. Cytoplasm {ECO:0000250|UniProtKB:O00422}. Nucleus speckle {ECO:0000250|UniProtKB:O00422}. Note=Shuttles between the nucleus and the cytoplasm (By similarity). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (By similarity). {ECO:0000250|UniProtKB:O00422}.
| null | null | null | null | null |
FUNCTION: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function (By similarity). {ECO:0000250, ECO:0000269|PubMed:22388736}.
|
Mus musculus (Mouse)
|
O55131
|
SEPT7_MOUSE
|
MSVSARSAAAEERSVNCGTMAQPKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEEEKANWEAQQRILEQQNSSRTLEKNKKKGKIF
| null | null |
cilium assembly [GO:0060271]; collateral sprouting [GO:0048668]; cortical cytoskeleton organization [GO:0030865]; cytoskeleton-dependent cytokinesis [GO:0061640]; dendritic spine morphogenesis [GO:0060997]; glucose import [GO:0046323]; mitotic cytokinesis [GO:0000281]; postsynapse organization [GO:0099173]; pseudopodium retraction [GO:0031270]; regulation of embryonic cell shape [GO:0016476]; spermatogenesis [GO:0007283]; vesicle-mediated transport [GO:0016192]
|
axon terminus [GO:0043679]; axoneme [GO:0005930]; cell cortex [GO:0005938]; cell division site [GO:0032153]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; kinetochore [GO:0000776]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; motile cilium [GO:0031514]; myelin sheath [GO:0043209]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic septin cytoskeleton [GO:0150050]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991]; septin complex [GO:0031105]; septin cytoskeleton [GO:0032156]; septin filament array [GO:0032160]; septin ring [GO:0005940]; spindle [GO:0005819]; synapse [GO:0045202]; vesicle [GO:0031982]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; molecular adaptor activity [GO:0060090]; structural constituent of postsynapse [GO:0099186]
|
PF00735;
|
3.40.50.300;
|
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17546647}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q16181}. Note=Distributed throughout the cytoplasm in prometaphase cells. Associated with the spindle during metaphase. Associated with the central spindle and at the cleavage furrow in anaphase cells. Detected at the midbody in telophase (By similarity). Associated with actin stress fibers. Found in the sperm annulus (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
| null | null | null | null | null |
FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
|
Mus musculus (Mouse)
|
O55134
|
PCD12_MOUSE
|
MMLLLPFLLGLLGPGSYLFISGDCQEVATVMVKFQVTEEVPSGTVIGKLSQELRVEERRGKAGDAFQILQLPQALPVQMNSEDGLLSTSSRLDREKLCRQEDPCLVSFDVLATGASALIHVEIQVLDINDHQPQFPKDEQELEISESASLHTRIPLDRALDQDTGPNSLYSYSLSPSEHFALDVIVGPDETKHAELVVVKELDRELHSYFDLVLTAYDNGNPPKSGISVVKVNVLDSNDNSPVFAESSLALEIPEDTVPGTLLINLTATDPDQGPNGEVEFFFGKHVSPEVMNTFGIDAKTGQIILRQALDYEKNPAYEVDVQARDLGPNSIPGHCKVLIKVLDVNDNAPSILITWASQTSLVSEDLPRDSFIALVSANDLDSGNNGLVHCWLNQELGHFRLKRTNGNTYMLLTNATLDREQWPIYTLTVFAQDQGPQPLSAEKELQIQVSDVNDNAPVFEKSRYEVSTWENNPPSLHLITLKAHDADLGSNGKVSYRIKDSPVSHLVIIDFETGEVTAQRSLDYEQMAGFEFQVIAEDRGQPQLASSISVWVSLLDANDNAPEVIQPVLSEGKATLSVLVNASTGHLLLPIENPSGMDPAGTGIPPKATHSPWSFLLLTIVARDADSGANGELFYSIQSGNDAHLFFLSPSLGQLFINVTNASSLIGSQWDLGIVVEDQGSPSLQTQVSLKVVFVTSVDHLRDSAHEPGVLSTPALALICLAVLLAIFGLLLALFVSICRTERKDNRAYNCREAESSYRHQPKRPQKHIQKADIHLVPVLRAHENETDEVRPSHKDTSKETLMEAGWDSCLQAPFHLTPTLYRTLRNQGNQGELAESQEVLQDTFNFLFNHPRQRNASRENLNLPESPPAVRQPLLRPLKVPGSPIARATGDQDKEEAPQSPPASSATLRRQRNFNGKVSPRGESGPHQILRSLVRLSVAAFAERNPVEEPAGDSPPVQQISQLLSLLHQGQFQPKPNHRGNKYLAKPGGSSRGTIPDTEGLVGLKPSGQAEPDLEEGPPSPEEDLSVKRLLEEELSSLLDPNTGLALDKLSPPDPAWMARLSLPLTTNYRDNLSSPDATTSEEPRTFQTFGKTVGPGPELSPTGTRLASTFVSEMSSLLEMLLGQHTVPVEAASAALRRLSVCGRTLSLDLATSGASASEAQGRKKAAESRLGCGRNL
| null | null |
calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell adhesion [GO:0007155]; glycogen metabolic process [GO:0005977]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; labyrinthine layer development [GO:0060711]
|
cell-cell junction [GO:0005911]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]
|
PF00028;PF08266;
|
2.60.40.60;
| null |
PTM: N-glycosylated. {ECO:0000269|PubMed:15541725}.; PTM: [Protocadherin-12]: Cleaved by ADAM10 close to the transmembrane domain to release the Protocadherin-12, secreted form in the serum. Cleavage results in reduced cellular adhesion in a cell migration assay. {ECO:0000250|UniProtKB:Q9NPG4}.
|
SUBCELLULAR LOCATION: [Protocadherin-12]: Cell membrane {ECO:0000250|UniProtKB:Q9NPG4}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000269|PubMed:9651350}.; SUBCELLULAR LOCATION: [Protocadherin-12, secreted form]: Secreted {ECO:0000250|UniProtKB:Q9NPG4}. Note=The secreted form is produced following cleavage by ADAM10. {ECO:0000250|UniProtKB:Q9NPG4}.
| null | null | null | null | null |
FUNCTION: Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions (PubMed:9651350). Acts as a regulator of cell migration, probably via increasing cell-cell adhesion (By similarity). Promotes homotypic calcium-dependent aggregation and adhesion and clusters at intercellular junctions (PubMed:9651350). Unable to bind to catenins, weakly associates with the cytoskeleton (PubMed:9651350). {ECO:0000250|UniProtKB:Q9NPG4, ECO:0000269|PubMed:9651350}.
|
Mus musculus (Mouse)
|
O55135
|
IF6_MOUSE
|
MAVRASFENNCEVGCFAKLTNAYCLVAIGGSENFYSVFEGELSDAIPVVHASIAGCRIIGRMCVGNRHGLLVPNNTTDQELQHIRNSLPDSVQIRRVEERLSALGNVTTCNDYVALVHPDLDRETEEILADVLKVEVFRQTVADQVLVGSYCVFSNQGGLVHPKTSIEDQDELSSLLQVPLVAGTVNRGSEVIAAGMVVNDWCAFCGLDTTSTELSVVESVFKLNEAKPSTIATSMRDSLIDSLT
| null | null |
assembly of large subunit precursor of preribosome [GO:1902626]; cytosolic ribosome assembly [GO:0042256]; maturation of 5.8S rRNA [GO:0000460]; maturation of LSU-rRNA [GO:0000470]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; miRNA-mediated post-transcriptional gene silencing [GO:0035195]; positive regulation of translation [GO:0045727]; regulation of fatty acid biosynthetic process [GO:0042304]; regulation of glycolytic process [GO:0006110]; regulation of megakaryocyte differentiation [GO:0045652]; regulation of reactive oxygen species metabolic process [GO:2000377]; response to insulin [GO:0032868]; ribosomal subunit export from nucleus [GO:0000054]
|
cytosol [GO:0005829]; intermediate filament [GO:0005882]; lamin filament [GO:0005638]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; preribosome, large subunit precursor [GO:0030687]; synapse [GO:0045202]
|
ribosomal large subunit binding [GO:0043023]; ribosome binding [GO:0043022]; translation initiation factor activity [GO:0003743]
|
PF01912;
| null |
EIF-6 family
|
PTM: Phosphorylation at Ser-174 and Ser-175 by CSNK1D/CK1 promotes nuclear export. {ECO:0000250|UniProtKB:P56537}.; PTM: Ufmylated by UFL1. {ECO:0000269|PubMed:28575669}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Shuttles between cytoplasm and nucleus/nucleolus.
| null | null | null | null | null |
FUNCTION: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-dependent protein kinase C activity. In tissues responsive to insulin, controls fatty acid synthesis and glycolysis by exerting translational control of adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR (PubMed:26383020). Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis (PubMed:26391622). Involved in miRNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (By similarity). Modulates cell cycle progression and global translation of pre-B cells, its activation seems to be rate-limiting in tumorigenesis and tumor growth (PubMed:21665150). {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000269|PubMed:18784653, ECO:0000269|PubMed:21665150, ECO:0000269|PubMed:26383020, ECO:0000269|PubMed:26391622}.
|
Mus musculus (Mouse)
|
O55137
|
ACOT1_MOUSE
|
MEATLNLEPSGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLVKRDVQTPFVVELEVLDGHEPDGGQRLAHAVHERHFLAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKNMETMHMEYFEEAVNYLRSHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTISYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVDKKSFIPVERSDTTFLFLVGQDDHNWKSEFYADEISKRLQAHGKEKPQIICYPAAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHAMAQLDAWQQLQTFFHKQLGSECLHVSPKI
|
3.1.2.-; 3.1.2.2
| null |
acyl-CoA metabolic process [GO:0006637]; fatty acid metabolic process [GO:0006631]; long-chain fatty acid metabolic process [GO:0001676]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
carboxylic ester hydrolase activity [GO:0052689]; fatty acyl-CoA hydrolase activity [GO:0047617]
|
PF08840;PF04775;
|
2.60.40.2240;3.40.50.1820;
|
C/M/P thioester hydrolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O88267}.
|
CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724; Evidence={ECO:0000305|PubMed:11694534};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for C16:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=15.2 uM for C10:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=2.6 uM for C12:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=3.5 uM for C14:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=0.5 uM for C20:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=1.5 uM for C14:1-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=1.1 uM for C16:1-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=2.4 uM for C18:1(cis)-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=1.8 uM for C18:1(trans)-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=4.5 uM for C18:2-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=3 uM for C20:4-acyl-CoA {ECO:0000269|PubMed:11694534}; Vmax=1.2 umol/min/mg enzyme with C16:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.192 umol/min/mg enzyme with C10:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.78 umol/min/mg enzyme with C12:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=1.68 umol/min/mg enzyme with C14:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.692 umol/min/mg enzyme with C18:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.245 umol/min/mg enzyme with C20:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.745 umol/min/mg enzyme with C14:1-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.621 umol/min/mg enzyme with C16:1-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.176 umol/min/mg enzyme with C18:1(cis)-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.188 umol/min/mg enzyme with C18:1(trans)-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.316 umol/min/mg enzyme with C18:2-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.007 umol/min/mg enzyme with C20:4-acyl-CoA as substrate {ECO:0000269|PubMed:11694534};
|
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:11694534}.
| null | null |
FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20). {ECO:0000269|PubMed:11694534}.
|
Mus musculus (Mouse)
|
O55142
|
RL35A_MOUSE
|
MSGRLWCKAIFAGYKRGLRNQREHTALLKIEGVYARDETEFYLGKRCAYVYKAKNNTVTPGGKPNKTRVIWGKVTRAHGNSGMVRAKFRSNLPAKAIGHRIRVMLYPSRI
| null | null |
cytoplasmic translation [GO:0002181]; ribosomal large subunit biogenesis [GO:0042273]; translation at postsynapse [GO:0140242]; translation at presynapse [GO:0140236]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; mitochondrion [GO:0005739]; postsynapse [GO:0098794]; presynapse [GO:0098793]; ribosome [GO:0005840]; synapse [GO:0045202]
|
structural constituent of ribosome [GO:0003735]
|
PF01247;
|
2.40.10.190;
|
Eukaryotic ribosomal protein eL33 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}.
| null | null | null | null | null |
FUNCTION: Component of the large ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). Required for the proliferation and viability of hematopoietic cells (By similarity). {ECO:0000250|UniProtKB:P18077, ECO:0000269|PubMed:36517592}.
|
Mus musculus (Mouse)
|
O55143
|
AT2A2_MOUSE
|
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDTCSLNEFSITGSTYAPIGEVQKDDKPVKCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTPGVKQKIMSVIREWGSGSDTLRCLALATHDNPLKREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELSPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKSEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFDGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNLTQWLMVLKISLPVILMDETLKFVARNYLEQPGKECVQPATKSSCSLSACTDGISWPFVLLIMPLVVWVYSTDTNFSDMFWS
|
7.2.2.10
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11607};
|
autophagosome assembly [GO:0000045]; autophagosome membrane docking [GO:0016240]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; calcium ion transport from cytosol to endoplasmic reticulum [GO:1903515]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to oxidative stress [GO:0034599]; ER-nucleus signaling pathway [GO:0006984]; intracellular calcium ion homeostasis [GO:0006874]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; negative regulation of heart contraction [GO:0045822]; neuron cellular homeostasis [GO:0070050]; organelle localization by membrane tethering [GO:0140056]; organelle organization [GO:0006996]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of endoplasmic reticulum calcium ion concentration [GO:0032470]; regulation of calcium ion-dependent exocytosis of neurotransmitter [GO:1903233]; regulation of cardiac muscle cell action potential involved in regulation of contraction [GO:0098909]; regulation of cardiac muscle cell membrane potential [GO:0086036]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of muscle contraction [GO:0006937]; regulation of the force of heart contraction [GO:0002026]; relaxation of cardiac muscle [GO:0055119]; response to peptide hormone [GO:0043434]; sarcoplasmic reticulum calcium ion transport [GO:0070296]; T-tubule organization [GO:0033292]; transition between fast and slow fiber [GO:0014883]
|
apical ectoplasmic specialization [GO:0061831]; endoplasmic reticulum [GO:0005783]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane bounded cell projection [GO:0120025]; protein-containing complex [GO:0032991]; ribbon synapse [GO:0097470]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; lncRNA binding [GO:0106222]; lutropin-choriogonadotropic hormone receptor binding [GO:0031775]; P-type calcium transporter activity [GO:0005388]; P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential [GO:0086039]; S100 protein binding [GO:0044548]; transmembrane transporter binding [GO:0044325]
|
PF13246;PF00689;PF00690;PF00122;PF00702;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily
|
PTM: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000269|PubMed:32116663}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23395171, ECO:0000269|PubMed:32973183}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:22355118}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000269|PubMed:32973183}.
|
CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000269|PubMed:28890335}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; Evidence={ECO:0000269|PubMed:28890335};
| null | null | null | null |
FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis. {ECO:0000250|UniProtKB:P16615, ECO:0000269|PubMed:22355118, ECO:0000269|PubMed:22971924, ECO:0000269|PubMed:32973183}.; FUNCTION: [Isoform 2]: Involved in the regulation of the contraction/relaxation cycle (PubMed:23395171). Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation (PubMed:23395171). Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation (PubMed:23395171). {ECO:0000269|PubMed:23395171}.
|
Mus musculus (Mouse)
|
O55144
|
TLX3_MOUSE
|
MEAPASAQTPHPHEPISFGIDQILNSPDQDSAPAPRGPDGASYLGGPPGGRPGAAYPSLPASFAGLGAPFEDAGSYSVNLSLAPAGVIRVPAHRPLPGAVPPPLPSALPAMPSVPTVSSLGGLNFPWMESSRRFVKDRFTAAAALTPFTVTRRIGHPYQNRTPPKRKKPRTSFSRVQICELEKRFHRQKYLASAERAALAKSLKMTDAQVKTWFQNRRTKWRRQTAEEREAERQQASRLMLQLQHDAFQKSLNDSIQPDPLCLHNSSLFALQNLQPWEEDSSKVPAVTSLV
| null | null |
animal organ development [GO:0048513]; central nervous system development [GO:0007417]; GABAergic neuron differentiation [GO:0097154]; negative regulation of neuron differentiation [GO:0045665]; neuron differentiation [GO:0030182]; neuron fate specification [GO:0048665]; neuron migration [GO:0001764]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; regulation of transcription by RNA polymerase II [GO:0006357]; respiratory gaseous exchange by respiratory system [GO:0007585]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
O55145
|
X3CL1_RAT
|
MAPSQLAWLLRLAAFFHLCTLLAGQHLGMTKCNITCHKMTSPIPVTLLIHYQLNQESCGKRAIILETRQHRHFCADPKEKWVQDAMKHLDHQTAALTRNGGKFEKRVDNVTPRITSATRGLSPTALAKPESATVEDLTLEPTAISQEARRPMGTSQEPPAAVTGSSPSTSKAQDAGLAAKPQSTGISEVAAVSTTIWPSSAVYQSGSSLWAEEKATESPPTIALSTQASTTSSPKQNVGSEGQPPWVQEQDSTPEKSPGPEETNPVHTDIFQDRGPGSTVHPSVAPTSSEKTPSPELVASGSQAPKVEEPIHATADPQKLSVFITPVPDSQAATRRQAVGLLAFLGLLFCLGVAMFAYQSLQGCPRKMAGEMVEGLRYVPRSCGSNSYVLVPV
| null | null |
angiogenesis involved in wound healing [GO:0060055]; autocrine signaling [GO:0035425]; cell adhesion [GO:0007155]; cell chemotaxis [GO:0060326]; cell-cell adhesion [GO:0098609]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; cytokine-mediated signaling pathway [GO:0019221]; eosinophil chemotaxis [GO:0048245]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; inhibitory postsynaptic potential [GO:0060080]; integrin activation [GO:0033622]; leukocyte migration involved in inflammatory response [GO:0002523]; lymphocyte chemotaxis [GO:0048247]; microglial cell activation [GO:0001774]; microglial cell proliferation [GO:0061518]; monocyte chemotaxis [GO:0002548]; negative regulation of apoptotic process [GO:0043066]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of cell migration [GO:0030336]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of glutamate receptor signaling pathway [GO:1900450]; negative regulation of hippocampal neuron apoptotic process [GO:0110091]; negative regulation of interleukin-1 alpha production [GO:0032690]; negative regulation of microglial cell activation [GO:1903979]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of vasoconstriction [GO:0045906]; neuron cellular homeostasis [GO:0070050]; neutrophil chemotaxis [GO:0030593]; positive chemotaxis [GO:0050918]; positive regulation of actin filament bundle assembly [GO:0032233]; positive regulation of calcium-independent cell-cell adhesion [GO:0051041]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of I-kappaB phosphorylation [GO:1903721]; positive regulation of inflammatory response [GO:0050729]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of microglial cell migration [GO:1904141]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta1 production [GO:0032914]; regulation of lipopolysaccharide-mediated signaling pathway [GO:0031664]; response to hypoxia [GO:0001666]; response to ischemia [GO:0002931]; wound healing [GO:0042060]
|
cell body [GO:0044297]; cell projection [GO:0042995]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]
|
CCR chemokine receptor binding [GO:0048020]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; CX3C chemokine receptor binding [GO:0031737]; CXCR1 chemokine receptor binding [GO:0045237]; integrin binding [GO:0005178]
|
PF00048;
|
2.40.50.40;
|
Intercrine delta family
|
PTM: A soluble short form may be released by proteolytic cleavage from the long membrane-anchored form. {ECO:0000250|UniProtKB:P78423}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P78423}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed fractalkine]: Secreted {ECO:0000250|UniProtKB:P78423}.
| null | null | null | null | null |
FUNCTION: Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1. The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis. Regulates leukocyte adhesion and migration processes at the endothelium. Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner. In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins. In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1. {ECO:0000250|UniProtKB:P78423}.; FUNCTION: [Processed fractalkine]: The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. {ECO:0000250|UniProtKB:P78423}.; FUNCTION: [Fractalkine]: The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. {ECO:0000250|UniProtKB:P78423}.
|
Rattus norvegicus (Rat)
|
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